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Start Over Author "Deacon, An" Journal proteins: structure, function, and bioinformatics
94 results on '"Deacon, An"'

1. Crystal structure of a putative quorum sensing-regulated protein (PA3611) from the Pseudomonas-specific DUF4146 family

Author

Debanu Das, Mark W. Knuth, Scott A. Lesley, Hsiu-Ju Chiu, Adam Godzik, Henry J Tien, Marc-André Elsliger, Joanna C Grant, Ian A. Wilson, Lukasz Jaroszewski, Ashley M. Deacon, Mitchell D. Miller, and Carol L. Farr

Subjects
Protein family, Pseudomonas aeruginosa, Computational biology, Biology, medicine.disease_cause, Biochemistry, Structural genomics, Microbiology, Conserved sequence, Quorum sensing, Structural Biology, medicine, Protein function prediction, Molecular Biology, Gene, Peptide sequence
Abstract

Pseudomonas aeruginosa is an opportunistic pathogen commonly found in humans and other organisms and is an important cause of infection especially in patients with compromised immune defense mechanisms. The PA3611 gene of P. aeruginosa PAO1 encodes a secreted protein of unknown function, which has been recently classified into a small Pseudomonas-specific protein family called DUF4146. As part of our effort to extend structural coverage of novel protein space and provide a structure-based functional insight into new protein families, we report the crystal structure of PA3611, the first structural representative of the DUF4146 protein family. Proteins 2014; 82:1086–1092. © 2013 Wiley Periodicals, Inc.

Published
2013
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2. Crystal structure of a member of a novel family of dioxygenases (PF10014) reveals a conserved cupin fold and active site

Author

Ashley M. Deacon, Mitchell D. Miller, Mark W. Knuth, Hsiu-Ju Chiu, Qingping Xu, Marc-André Elsliger, Ian A. Wilson, Joanna C Grant, Carol L. Farr, Scott A. Lesley, Lukasz Jaroszewski, and Adam Godzik

Subjects
Structural similarity, Biofilm, Active site, Biology, Biochemistry, Conserved sequence, Hydroxylation, chemistry.chemical_compound, Biosynthesis, chemistry, Structural Biology, biology.protein, Molecular Biology, Peptide sequence, Conformational isomerism
Abstract

PF10014 is a novel family of 2-oxyglutarate-Fe(2+) -dependent dioxygenases that are involved in biosynthesis of antibiotics and regulation of biofilm formation, likely by catalyzing hydroxylation of free amino acids or other related ligands. The crystal structure of a PF10014 member from Methylibium petroleiphilum at 1.9 A resolution shows strong structural similarity to cupin dioxygenases in overall fold and active site, despite very remote homology. However, one of the β-strands of the cupin catalytic core is replaced by a loop that displays conformational isomerism that likely regulates the active site.

Published
2013
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3. Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima

Author

Marc-André Elsliger, Qingping Xu, Mark Levisson, Sjon Hendriks, Frank von Delft, Gye Won Han, Pietro Roversi, Marc C. Deller, Daniel McMullan, Scott A. Lesley, Ashley M. Deacon, Servé W. M. Kengen, Ian A. Wilson, Lynn F. Ten Eyck, Mitchell D. Miller, Peter Biely, Andreas Kreusch, John van der Oost, and Claus Flensburg

Subjects
biology, Stereochemistry, Acetylesterase, Cephalosporin C, Random hexamer, biology.organism_classification, Biochemistry, Esterase, Serine, chemistry.chemical_compound, chemistry, Structural Biology, Acetylation, Thermotoga maritima, Hydrolase, Molecular Biology
Abstract

TM0077 from Thermotoga maritima is a member of the carbohydrate esterase family 7 and is active on a variety of acetylated compounds, including cephalosporin C. TM0077 esterase activity is confined to short-chain acyl esters (C2-C3), and is optimal around 100°C and pH 7.5. The positional specificity of TM0077 was investigated using 4-nitrophenyl-β-D-xylopyranoside monoacetates as substrates in a β-xylosidase-coupled assay. TM0077 hydrolyzes acetate at positions 2, 3, and 4 with equal efficiency. No activity was detected on xylan or acetylated xylan, which implies that TM0077 is an acetyl esterase and not an acetyl xylan esterase as currently annotated. Selenomethionine-substituted and native structures of TM0077 were determined at 2.1 and 2.5 A resolution, respectively, revealing a classic α/β-hydrolase fold. TM0077 assembles into a doughnut-shaped hexamer with small tunnels on either side leading to an inner cavity, which contains the six catalytic centers. Structures of TM0077 with covalently bound phenylmethylsulfonyl fluoride and paraoxon were determined to 2.4 and 2.1 A, respectively, and confirmed that both inhibitors bind covalently to the catalytic serine (Ser188). Upon binding of inhibitor, the catalytic serine adopts an altered conformation, as observed in other esterase and lipases, and supports a previously proposed catalytic mechanism in which Ser hydroxyl rotation prevents reversal of the reaction and allows access of a water molecule for completion of the reaction.

Published
2012
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4. Genomics, evolution, and crystal structure of a new family of bacterial spore kinases

Author

Gerard Manning, Ian A. Wilson, Hsiu-Ju Chiu, Mitchell D. Miller, Herbert L. Axelrod, Eric D. Scheeff, and Ashley M. Deacon

Subjects
Genetics, 0303 health sciences, biology, 030306 microbiology, Kinase, fungi, Bacillus, Bacillus subtilis, biology.organism_classification, Biochemistry, Conserved sequence, 03 medical and health sciences, Structural Biology, Phylogenetics, Bacterial spore, Molecular Biology, Peptide sequence, Function (biology), 030304 developmental biology
Abstract

Bacterial spore formation is a complex process of fundamental relevance to biology and human disease. The spore coat structure is complex and poorly understood, and the roles of many of the protein components remain unclear. We describe a new family of spore coat proteins, the bacterial spore kinases (BSKs), and the first crystal structure of a BSK, YtaA (CotI) from Bacillus subtilis. BSKs are widely distributed in spore-forming Bacillus and Clostridium species, and have a dynamic evolutionary history. Sequence and structure analyses indicate that the BSKs are CAKs, a prevalent group of small molecule kinases in bacteria that is distantly related to the eukaryotic protein kinases. YtaA has substantial structural similarity to CAKs, but also displays distinctive features that broaden our understanding of the CAK group. Evolutionary constraint analysis of the protein surfaces indicates that members of the BSK family have distinct clade-conserved patterns in the substrate binding region, and probably bind and phosphorylate distinct targets. Several classes of BSKs have apparently independently lost catalytic activity to become pseudokinases, indicating that the family also has a major noncatalytic function. Proteins 2010. © 2009 Wiley-Liss, Inc.

Published
2009
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5. Crystal structure of a novel Sm-like protein of putative cyanophage origin at 2.60 Å resolution

Author

Lukasz Jaroszewski, Ashley M. Deacon, Julie Feuerhelm, Hsiu-Ju Chiu, Debanu Das, Dana Weekes, Jessica Paulsen, Qingping Xu, Marc C. Deller, Piotr Kozbial, Ian A. Wilson, Christina Puckett, Gye Won Han, Silvya Oommachen, Abhinav Kumar, Marc André Elsliger, Amanda Nopakun, Natasha Sefcovic, Linda Okach, Edward Nigoghossian, Herbert L. Axelrod, Keith O. Hodgson, Dennis Carlton, Scott A. Lesley, Mark W. Knuth, Heath E. Klock, Henry Tien, Carol L. Farr, Kevin D. Murphy, Hope A. Johnson, Slawomir K. Grzechnik, Kevin K. Jin, Henry van den Bedem, Ylva Elias, Adam Godzik, Dustin C. Ernst, Tamara Astakhova, Andrew T. Morse, Aprilfawn White, Thomas Clayton, John Wooley, Connie Chen, Christine B Trame, Daniel McMullan, Christina V. Trout, Joanna Hale, Ron Reyes, Claire Acosta, David Marciano, Polat Abdubek, Lian Duan, Sanjay Krishna, Christopher L. Rife, Prasad Burra, Sebastian Sudek, Mitchell D. Miller, and Anna Grzechnik

Subjects
Genetics, Viral protein, RNA, Cyanophage, RNA-binding protein, Biology, medicine.disease_cause, Biochemistry, Structural genomics, Protein structure, Structural Biology, Nucleic acid, medicine, Molecular Biology, Peptide sequence
Abstract

ECX21941 represents a very large family (over 600 members) of novel, ocean metagenome-specific proteins identified by clustering of the dataset from the Global Ocean Sampling expedition. The crystal structure of ECX21941 reveals unexpected similarity to Sm/LSm proteins, which are important RNA-binding proteins, despite no detectable sequence similarity. The ECX21941 protein assembles as a homopentamer in solution and in the crystal structure when expressed in Escherichia coli and represents the first pentameric structure for this Sm/LSm family of proteins, although the actual oligomeric form in vivo is currently not known. The genomic neighborhood analysis of ECX21941 and its homologs combined with sequence similarity searches suggest a cyanophage origin for this protein. The specific functions of members of this family are unknown, but our structure analysis of ECX21941 indicates nucleic acid-binding capabilities and suggests a role in RNA and/or DNA processing.

Published
2008
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6. Crystal structure of the Fic (Filamentation induced by cAMP) family protein SO4266 (gi|24375750) from Shewanella oneidensis MR-1 at 1.6 Å resolution

Author

Henry Tien, Keith O. Hodgson, Aprilfawn White, Linda Okach, Tamara Astakhova, Marc-André Elsliger, Qingping Xu, Edward Nigoghossian, Julie Feuerhelm, Kevin K. Jin, Dustin C. Ernst, Andrew T. Morse, Christine B Trame, Henry van den Bedem, Slawomir K. Grzechnik, Prasad Burra, Abhinav Kumar, Hsiu-Ju Chiu, Herbert L. Axelrod, Heath E. Klock, Thomas Clayton, David Marciano, Polat Abdubek, Gye Won Han, Marc C. Deller, Dennis Carlton, Christina V. Trout, Joanna Hale, Silvya Oommachen, Ashley M. Deacon, Natasha Sefcovic, Debanu Das, Scott A. Lesley, Sanjay Krishna, Lukasz Jaroszewski, Ylva Elias, Ian A. Wilson, Mitchell D. Miller, Anna Grzechnik, Christopher L. Rife, Daniel McMullan, John Wooley, Claire Acosta, Piotr Kozbial, Kevin D. Murphy, Mark W. Knuth, Adam Godzik, Dana Weekes, Lian Duan, Ron Reyes, and Jessica Paulsen

Subjects
Shewanella, Protein family, Protein Conformation, Protein subunit, Amino Acid Motifs, Molecular Sequence Data, Protein Data Bank (RCSB PDB), Biology, Crystallography, X-Ray, Biochemistry, DNA-binding protein, Article, Structural genomics, Protein structure, Bacterial Proteins, Structural Biology, Amino Acid Sequence, Molecular Biology, DNA, DNA-binding domain, computer.file_format, Protein Data Bank, Protein Structure, Tertiary, Dimerization, computer, Protein Binding
Abstract

The protein SO4266 (gi|24375750) from the bacterium Shewanella oneidensis MR-1 is annotated as a member of Pfam PF02661. This family consists of Fic (filamentation induced by cAMP) proteins and their relatives, and is characterized by the presence of a well-conserved HPFXXGNG motif 1. The biochemistry of Fic proteins has not been characterized extensively and their exact molecular functions remain unknown. From early studies in Escherichia coli, it is believed that Fic proteins and cAMP may be involved in a regulatory mechanism of cell division, including folate metabolism by the synthesis of p-aminobenzoic acid (PABA) or folate 1. Proteins containing the Fic domain are present in all kingdoms of life and range in size from ~200 to 500 amino acids. The Fic protein family contains 647 members, including two human proteins, according to Pfam (May 2008). Sequence-based clustering 2 of this protein family, at 30% sequence identity, groups these proteins into 18 clusters. Three crystal structures of Fic proteins from bacteria (unpublished) are available in the Protein Data Bank [accession codes 2g03 (194 residues, 2.2 A), 2f6s (201 residues, 2.5 A) and 3cuc (262 residues, 2.7 A)]. The first two of these proteins belong to a single cluster of 16 members and share ~60% sequence identity. The anti-apoptotic bacterial effector protein BepA, which is a type IV secretion (T4S) system substrate, also contains an N-terminal Fic domain 3. In humans, the Fic domain is present in the Huntingtin Interacting Protein E (HYPE; Uniprot entry Q9BVA6_HUMAN), a protein of unknown function that is thought to interact with Huntingtin, one of the major proteins in the Huntington's disease protein interaction network (listed as NAD- or FAD-binding) 4. Bioinformatics analysis of prokaryotic toxin-antitoxin networks 5 suggests that Fic proteins are putative death-on-curing (Doc) toxins that are part of the Phd-Doc system. These proteins likely function as metal-dependent nucleases or RNA-processing enzymes, 5 while more recent studies suggest that Doc toxicity is caused by inhibition of translation elongation 6. SO4266 (Uniprot entry Q8E9K5_SHEON), at 372 amino acids, is one of the largest Fic domain-containing proteins to have its structure determined. Interestingly, both HYPE and SO4266 belong to the largest sequence cluster in this family (n.b. our B. thetaiotaomicron {"type":"entrez-protein","attrs":{"text":"NP_811426.1","term_id":"29347923","term_text":"NP_811426.1"}}NP_811426.1 structure with PDB id 3cuc also belongs to this cluster), which comprises 466 out of 647 proteins, and share ~32% sequence identity in the Fic domain. Here, we report the crystal structure of the SO4266 protein at 1.6 A resolution. The structure reveals a dimeric protein with additional electron density in the vicinity of the highly conserved HPFXXGNG motif in the Fic domain of one subunit that corresponds to the N-terminus of a symmetry-related molecule. In addition, the study also reveals a C-terminal winged-helix DNA-binding domain that sets it apart from the other Fic protein structures. The structure presented here is a representative of the largest sequence cluster and together with the structures of the other Fic proteins paves the way for further structure-based functional characterization.

Published
2008
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7. Crystal structure of a novel archaeal AAA+ ATPase SSO1545 from Sulfolobus solfataricus

Author

John Wooley, Mark W. Knuth, Ashley M. Deacon, Lukasz Jaroszewski, Ian A. Wilson, Thomas Clayton, Hsiu-Ju Chiu, Lian Duan, Abhinav Kumar, Adam Godzik, Scott A. Lesley, Gye Won Han, Kevin K. Jin, Marc-André Elsliger, Joanna Hale, Silvya Oommachen, Edward Nigoghossian, Keith O. Hodgson, Heath E. Klock, Slawomir K. Grzechnik, Qingping Xu, Julie Feuerhelm, Mitchell D. Miller, Henry van den Bedem, Dennis Carlton, Christopher L. Rife, Ron Reyes, Andrew T. Morse, Jessica Paulsen, Linda Okach, Tamara Astakhova, Daniel McMullan, Polat Abdubek, and Sanjay Krishna

Subjects
ved/biology, Sulfolobus solfataricus, ved/biology.organism_classification_rank.species, Biology, Biochemistry, AAA proteins, Structural genomics, Protein structure, Structural Biology, NAIP, Sequence motif, Molecular Biology, Peptide sequence, Protein Structure Initiative
Abstract

Signal transduction ATPases with numerous domains (STAND), a large class of P-loop NTPases, belong to AAA+ ATPases. They include AP(apoptotic)-ATPases (e.g., animal apoptosis regulators CED4/Apaf-1, plant disease resistance proteins, and bacterial AfsR-like transcription regulators), NACHT NTPases (e.g. CARD4, NAIP, Het-E-1, TLP1), and several other less well-characterized families. STAND differ from other P-loop NTPases by their unique sequence motifs, which include an hhGRExE (h, hydrophobic; x, any residue) motif at the N-terminal region, a GxP/GxxP motif at the C-terminal region of the NTPase domain, in addition to a C-terminal helical domain and additional domains such as WD40, TPR, LRR or catalytic modules. Despite significant biological interests, structural coverage of STAND proteins is very limited and only two other structures are currently known: the cell death regulators Apaf-1 and CED-4. Here, we report the crystal structure of SSO1545 from Sulfolobus solfataricus, which was determined using the semi-automated, high-throughput pipeline of the Joint Center for Structural Genomics (JCSG; http://www.jcsg.org), as part of the National Institute of General Medical Sciences' Protein Structure Initiative (PSI). SSO1545 (NP-342973.1), a representative of the archaeal STANDs, is a member of Pfam PF01637 and encodes a protein of 356 residues with calculated molecular weight and isoelectric point of 41.7more » kD and 8.2, respectively.« less

Published
2008
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8. Crystal structures of MW1337R and lin2004: Representatives of a novel protein family that adopt a four-helical bundle fold

Author

Abhinav Kumar, Ron Reyes, Henry van den Bedem, Marc André Elsliger, Aprilfawn White, Scott A. Lesley, Ian A. Wilson, Keith O. Hodgson, Guenter Wolf, Linda Okach, David Marciano, Edward Nigoghossian, Piotr Kozbial, Christopher L. Rife, Chloe Zubieta, Ylva Elias, Eric Koesema, Ashley M. Deacon, Glen Spraggon, Kevin K. Jin, Kevin D. Murphy, Herbert L. Axelrod, Hsiu-Ju Chiu, Andrew T. Morse, Mitchell D. Miller, Dennis Carlton, Mark W. Knuth, Adam Godzik, Gye Won Han, Silvya Oommachen, John Wooley, Thomas Clayton, Christina V. Trout, Dana Weekes, Lian Duan, Daniel McMullan, Joanna Hale, Tamara Astakhova, Polat Abdubek, Sanjay Krishna, Claire Acosta, Slawomir K. Grzechnik, Lukasz Jaroszewski, Julie Feuerhelm, Marc C. Deller, Qingping Xu, and Heath E. Klock

Subjects
Genetics, Protein Folding, Accession number (library science), Operon, Molecular Sequence Data, Bacillus subtilis, Biology, Crystallography, X-Ray, biology.organism_classification, Biochemistry, Protein Structure, Secondary, Protein Structure, Tertiary, Structural genomics, chemistry.chemical_compound, Protein structure, Bacterial Proteins, chemistry, Structural Biology, Complementary DNA, Amino Acid Sequence, Molecular Biology, Gene, DNA
Abstract

To extend the structural coverage of proteins with unknown functions, we targeted a novel protein family (Pfam accession number PF08807, DUF1798) for which we proposed and determined the structures of two representative members. The MW1337R gene of Staphylococcus aureus subsp. aureus Rosenbach (Wood 46) encodes a protein with a molecular weight of 13.8 kDa (residues 1-116) and a calculated isoelectric point of 5.15. The lin2004 gene of the nonspore-forming bacterium Listeria innocua Clip11262 encodes a protein with a molecular weight of 14.6 kDa (residues 1-121) and a calculated isoelectric point of 5.45. MW1337R and lin2004, as well as their homologs, which, so far, have been found only in Bacillus, Staphylococcus, Listeria, and related genera (Geobacillus, Exiguobacterium, and Oceanobacillus), have unknown functions and are annotated as hypothetical proteins. The genomic contexts of MW1337R and lin2004 are similar and conserved in related species. In prokaryotic genomes, most often, functionally interacting proteins are coded by genes, which are colocated in conserved operons. Proteins from the same operon as MW1337R and lin2004 either have unknown functions (i.e., belong to DUF1273, Pfam accession number PF06908) or are similar to ypsB from Bacillus subtilis. The function of ypsB is unclear, although it has a strong similaritymore » to the N-terminal region of DivIVA, which was characterized as a bifunctional protein with distinct roles during vegetative growth and sporulation. In addition, members of the DUF1273 family display distant sequence similarity with the DprA/Smf protein, which acts downstream of the DNA uptake machinery, possibly in conjunction with RecA. The RecA activities in Bacillus subtilis are modulated by RecU Holliday-junction resolvase. In all analyzed cases, the gene coding for RecU is in the vicinity of MW1337R, lin2004, or their orthologs, but on a different operon located in the complementary DNA strand. Here, we report the crystal structures of MW1337R and lin2004, which were determined using the semiautomated, high-throughput pipeline of the Joint Center for Structural Genomics (JCSG), part of the National Institute of General Medical Sciences Protein Structure Initiative.« less

Published
2008
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9. Crystal structure of an ADP-ribosylated protein with a cytidine deaminase-like fold, but unknown function (TM1506), from Thermotoga maritima at 2.70 Å resolution

Author

Aprilfawn White, Jessica Paulsen, Polat Abdubek, Michael DiDonato, Sanjay Krishna, John Wooley, Daniel McMullan, Lian Duan, Andrew T. Morse, Henry van den Bedem, Christopher L. Rife, Slawomir K. Grzechnik, Mitchell D. Miller, Hsiu-Ju Chiu, Julie Feuerhelm, Keith O. Hodgson, Heath E. Klock, Marc-André Elsliger, Edward Nigoghossian, Thomas Clayton, Herbert L. Axelrod, Joanna Hale, Lukasz Jaroszewski, Qingping Xu, Scott A. Lesley, Piotr Kozbial, Ron Reyes, Scott M. Brittain, Ashley M. Deacon, Ian A. Wilson, Scott B. Ficarro, Adam Godzik, and Gye Won Han

Subjects
Biochemistry, Structural Biology, Thermophile, Thermotoga maritima, Posttranslational modification, Cytidine deaminase, Crystal structure, Biology, biology.organism_classification, Molecular Biology, Structural genomics
Published
2008
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10. Crystal structure of AICAR transformylase IMP cyclohydrolase (TM1249) fromThermotoga maritima at 1.88 Å resolution

Author

Lukasz Jaroszewski, Keith O. Hodgson, Marc-André Elsliger, John Wooley, Edward Nigoghossian, Andrew T. Morse, Scott A. Lesley, Tamara Astakhova, Jessica Paulsen, Guenter Wolf, Ron Reyes, Henry van den Bedem, Polat Abdubek, Aprilfawn White, Gye Won Han, Sanjay Krishna, Adam Godzik, Hsiu-Ju Chiu, Mitchell D. Miller, Silvya Oommachen, Qingping Xu, Daniel McMullan, Christopher L. Rife, Slawomir K. Grzechnik, Herbert L. Axelrod, Thomas Clayton, Joanna Hale, Eric Koesema, Heath E. Klock, Lian Duan, Julie Feuerhelm, Ashley M. Deacon, Ian A. Wilson, Eileen Ambing, Dennis Carlton, Mark W. Knuth, Kevin Quijano, Dana Weekes, Kevin K. Jin, Justin Haugen, and Linda Okach

Subjects
Hydroxymethyl and Formyl Transferases, Models, Molecular, Binding Sites, Materials science, AICAR TRANSFORMYLASE/IMP CYCLOHYDROLASE, biology, Stereochemistry, Molecular Sequence Data, Resolution (electron density), Crystal structure, Crystallography, X-Ray, Multienzyme complexes, biology.organism_classification, Biochemistry, Multienzyme Complexes, Nucleotide Deaminases, Structural Biology, Thermotoga maritima, Phosphofructokinase 2, Amino Acid Sequence, Crystallization, Purine metabolism, Molecular Biology
Published
2008
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11. Crystal structure of 2-keto-3-deoxygluconate kinase (TM0067) fromThermotoga maritimaat 2.05 Å resolution

Author

Timothy M. McPhillips, Kevin Quijano, Andreas Kreusch, Scott A. Lesley, Guenter Wolf, Henry van den Bedem, Irimpan I. Mathews, Andrew T. Morse, Lukasz Jaroszewski, Mitchell D. Miller, Dana Weekes, Christopher L. Rife, Marc-André Elsliger, Peter Kuhn, Ashley M. Deacon, Daniel McMullan, Adam Godzik, Ross Floyd, Robert Schwarzenbacher, Ian A. Wilson, Jaume M. Canaves, Keith O. Hodgson, Eric Koesema, John S. Kovarik, Heath E. Klock, Glen Spraggon, John Wooley, Raymond C. Stevens, and Slawomir K. Grzechnik

Subjects
biology, Structural Biology, Stereochemistry, Chemistry, Thermotoga maritima, Resolution (electron density), Transferase, 2-keto-3-deoxygluconate kinase, Crystal structure, biology.organism_classification, Molecular Biology, Biochemistry
Published
2007
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12. Crystal structure of MtnX phosphatase fromBacillus subtilisat 2.0 Å resolution provides a structural basis for bipartite phosphomonoester hydrolysis of 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate

Author

Slawomir K. Grzechnik, Qingping Xu, Herbert L. Axelrod, Heath E. Klock, Aprilfawn White, Henry van den Bedem, John Wooley, Robert Schwarzenbacher, Guenter Wolf, Ian A. Wilson, Eric Koesema, Keith O. Hodgson, Justin Haugen, Polat Abdubek, Hsiu-Ju Chiu, Linda Okach, Sanjay Agarwalla, Christopher L. Rife, Ron Reyes, Andrew T. Morse, Eileen Ambing, Dennis Carlton, Sanjay Krishna, Mark W. Knuth, Mitchell D. Miller, Gye Won Han, Silvya Oommachen, Michael DiDonato, Marc-André Elsliger, Edward Nigoghossian, Eric Hampton, Lukasz Jaroszewski, Kumar Singh Saikatendu, Julie Feuerhelm, Jessica Paulsen, Thomas Clayton, Joanna Hale, Ashley M. Deacon, Adam Godzik, Daniel McMullan, Tamara Astakhova, Kevin K. Jin, Scott A. Lesley, and Lian Duan

Subjects
biology, Resolution (mass spectrometry), Chemistry, Stereochemistry, Hydrolysis, Molecular Sequence Data, Phosphatase, Crystal structure, Bacillus subtilis, Crystallography, X-Ray, biology.organism_classification, Phosphate, Biochemistry, Organophosphates, Phosphoric Monoester Hydrolases, chemistry.chemical_compound, Crystallography, Bacterial Proteins, Thioglycosides, Structural Biology, Hydrolase, Amino Acid Sequence, Molecular Biology
Published
2007
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13. Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA

Author

Chloe Zubieta, Abhinav Kumar, Keith O. Hodgson, Aprilfawn White, Mark W. Knuth, Polat Abdubek, Rosanne Joseph, Marc C. Deller, David Marciano, Heath E. Klock, Sanjay Krishna, Lian Duan, Hsiu-Ju Chiu, Slawomir K. Grzechnik, Scott A. Lesley, Henry van den Bedem, Paul Schimmel, Linda Okach, Gye Won Han, Silvya Oommachen, John Wooley, Christopher L. Rife, Mitchell D. Miller, Claire Acosta, Marc-André Elsliger, Edward Nigoghossian, Daniel McMullan, Mili Kapoor, Dana Weekes, Herbert L. Axelrod, Ylva Elias, Dennis Carlton, Lukasz Jaroszewski, Thomas Clayton, Tamara Astakhova, Julie Feuerhelm, Christina V. Trout, Kevin K. Jin, Joanna Hale, Qingping Xu, Ashley M. Deacon, Ian A. Wilson, Andrew T. Morse, Kevin D. Murphy, Adam Godzik, Piotr Kozbial, and Ron Reyes

Subjects
Shewanella, Heme binding, Stereochemistry, Molecular Sequence Data, Heme, Crystallography, X-Ray, Biochemistry, Structural genomics, chemistry.chemical_compound, Bacterial Proteins, Multienzyme Complexes, Structural Biology, Amino Acid Sequence, Binding site, Coloring Agents, Molecular Biology, Peptide sequence, Dye decolorizing peroxidase, Binding Sites, biology, Active site, Peroxidases, chemistry, biology.protein, Protein Binding, Peroxidase
Abstract

TyrA is a member of the dye-decolorizing peroxidase (DyP) family, a new family of heme-dependent peroxidase recently identified in fungi and bacteria. Here, we report the crystal structure of TyrA in complex with iron protoporphyrin (IX) at 2.3 A. TyrA is a dimer, with each monomer exhibiting a two-domain, alpha/beta ferredoxin-like fold. Both domains contribute to the heme-binding site. Co-crystallization in the presence of an excess of iron protoporphyrin (IX) chloride allowed for the unambiguous location of the active site and the specific residues involved in heme binding. The structure reveals a Fe-His-Asp triad essential for heme positioning, as well as a novel conformation of one of the heme propionate moieties compared to plant peroxidases. Structural comparison to the canonical DyP family member, DyP from Thanatephorus cucumeris (Dec 1), demonstrates conservation of this novel heme conformation, as well as residues important for heme binding. Structural comparisons with representative members from all classes of the plant, bacterial, and fungal peroxidase superfamily demonstrate that TyrA, and by extension the DyP family, adopts a fold different from all other structurally characterized heme peroxidases. We propose that a new superfamily be added to the peroxidase classification scheme to encompass the DyP family of heme peroxidases.

Published
2007
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14. Crystal structure of homoserine O-succinyltransferase from Bacillus cereus at 2.4 Å resolution

Author

Lukasz Jaroszewski, Abhinav Kumar, John Wooley, Herbert L. Axelrod, Sanjay Agarwalla, Dennis Carlton, Adam Godzik, Marc-André Elsliger, Hsiu-Ju Chiu, Edward Nigoghossian, Dana Weekes, Daniel McMullan, Keith O. Hodgson, Justin Haugen, Ashley M. Deacon, Mitchell D. Miller, Henry van den Bedem, Mark W. Knuth, Polat Abdubek, Thomas Clayton, Christopher L. Rife, Heath E. Klock, Sanjay Krishna, Qingping Xu, Marc C. Deller, Joanna Hale, Slawomir K. Grzechnik, Scott A. Lesley, Ian A. Wilson, Tamara Astakhova, Lian Duan, Eileen Ambing, Ron Reyes, Kevin K. Jin, Aprilfawn White, Eric Koesema, Andrew T. Morse, Gye Won Han, Silvya Oommachen, Michael DiDonato, David Marciano, Eric Hampton, and Chloe Zubieta

Subjects
Models, Molecular, biology, Protein Conformation, Chemistry, Stereochemistry, Extramural, Molecular Sequence Data, Resolution (electron density), Bacillus cereus, Homoserine O-Succinyltransferase, Crystal structure, Crystallography, X-Ray, biology.organism_classification, Haemophilus influenzae, Biochemistry, Microbiology, Bacterial Proteins, Structural Biology, Homoserine Transsuccinylase, Amino Acid Sequence, Dimerization, Molecular Biology
Published
2007
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15. Crystal structure of a transcription regulator (TM1602) from Thermotoga maritima at 2.3 Å resolution

Author

Jaume M. Canaves, Ian A. Wilson, John Wooley, Claire Acosta, John S. Kovarik, Guenter Wolf, Timothy M. McPhillips, Glen Spraggon, Dana Weekes, Scott A. Lesley, Adam Godzik, Slawomir K. Grzechnik, Mitchell D. Miller, Henry van den Bedem, Daniel McMullan, Andreas Kreusch, Lukasz Jaroszewski, Sanjay Krishna, Kevin Quijano, Keith O. Hodgson, Ashley M. Deacon, Eric Koesema, Marc-André Elsliger, Andrew T. Morse, Ross Floyd, and Heath E. Klock

Subjects
Models, Molecular, biology, Computer science, Stereochemistry, Molecular Sequence Data, Crystal structure, Crystallography, X-Ray, biology.organism_classification, Biochemistry, DNA-Binding Proteins, Structural Biology, Transcription (biology), Thermotoga maritima, Amino Acid Sequence, Crystallization, Molecular Biology, Transcription regulator, Transcription Factors
Published
2007
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16. Crystal structure of a glycerate kinase (TM1585) from Thermotoga maritima at 2.70 Å resolution reveals a new fold

Author

Ian A. Wilson, Guenter Wolf, Jaume M. Canaves, Keith O. Hodgson, John Wooley, Robert Schwarzenbacher, Andrew T. Morse, Peter Kuhn, Kevin Quijano, Andreas Kreusch, Sanjay Krishna, Marc-André Elsliger, Ross Floyd, Ashley M. Deacon, Glen Spraggon, Slawomir K. Grzechnik, Mitchell D. Miller, Timothy M. McPhillips, Eric Koesema, Daniel McMullan, Henry van den Bedem, Lukasz Jaroszewski, Scott A. Lesley, Adam Godzik, Qingping Xu, Raymond C. Stevens, John S. Kovarik, and Heath E. Klock

Subjects
Protein Folding, biology, Stereochemistry, Chemistry, Molecular Sequence Data, Fold (geology), Crystal structure, Crystallography, X-Ray, biology.organism_classification, Biochemistry, Phosphotransferases (Alcohol Group Acceptor), Bacterial Proteins, Structural Biology, Thermotoga maritima, Transferase, Amino Acid Sequence, Crystallization, Molecular Biology, Glycerate kinase
Published
2006
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17. Crystal structure of the ApbE protein (TM1553) from Thermotoga maritima at 1.58 Å resolution

Author

Peter Kuhn, Raymond C. Stevens, Keith O. Hodgson, Sanjay Agarwalla, Jaume M. Canaves, Marc-André Elsliger, Edward Nigoghossian, Henry van den Bedem, Jie Ouyang, Michael DiDonato, Heath E. Klock, Mitchell D. Miller, Mark W. Knuth, Kevin Quijano, Robert Schwarzenbacher, Guenter Wolf, Eric Koesema, Kin Moy, Aprilfawn White, Gye Won Han, Polat Abdubek, Kevin K. Jin, Eric Hampton, Scott M. Brittain, Slawomir K. Grzechnik, Sanjay Krishna, Xianhong Wang, Bill West, Scott A. Lesley, Hsiu-Ju Chiu, Herbert L. Axelrod, Justin Haugen, Jeff Velasquez, Andrew T. Morse, Daniel McMullan, Adam Godzik, Christopher L. Rife, Lukasz Jaroszewski, Joanna Hale, Tamara Astakhova, Ron Reyes, Sylvia Oommachen, John Wooley, Qingping Xu, Andreas Kreusch, Glen Spraggon, Jessica Paulsen, Ashley M. Deacon, Krzysztof Ginalski, Ian A. Wilson, and Eileen Ambing

Subjects
Materials science, biology, Lipoproteins, Molecular Sequence Data, Resolution (electron density), Crystal structure, Crystallography, X-Ray, biology.organism_classification, Biochemistry, Crystallography, Bacterial Proteins, Structural Biology, Thermotoga maritima, Amino Acid Sequence, Crystallization, Sequence Alignment, Molecular Biology
Published
2006
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18. Crystal structure of phosphoribosylformylglycinamidine synthase II (smPurL) from Thermotoga maritima at 2.15 Å resolution

Author

Glen Spraggon, John Wooley, Jeff Velasquez, Kevin Quijano, Daniel McMullan, Inna Levin, Marc-André Elsliger, Slawomir K. Grzechnik, Edward Nigoghossian, Robert Schwarzenbacher, Ian A. Wilson, Guenter Wolf, Gye Won Han, Adam Godzik, Eileen Ambing, Keith O. Hodgson, Jaume M. Canaves, Ron Reyes, Carina Grittini, Mitchell D. Miller, Peter Kuhn, Henry van den Bedem, Ashley M. Deacon, Eric Hampton, Polat Abdubek, Lukasz Jaroszewski, Aprilfawn White, Justin Haugen, Jessica Paulsen, Eric Koesema, Qingping Xu, Hsiu-Ju Chiu, Andreas Kreusch, Joanna Hale, S. Sri Krishna, Scott A. Lesley, Irimpan I. Mathews, Raymond C. Stevens, Heath E. Klock, Kin Moy, and Michael DiDonato

Subjects
Models, Molecular, chemistry.chemical_classification, DNA ligase, Binding Sites, Molecular Sequence Data, Resolution (electron density), Crystal structure, Biology, Crystallography, X-Ray, biology.organism_classification, Biochemistry, Phosphoribosylformylglycinamidine synthase, Protein Structure, Tertiary, Crystallography, chemistry, Structural Homology, Protein, Structural Biology, Thermotoga maritima, biology.protein, Amino Acid Sequence, Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor, Protein Structure, Quaternary, Molecular Biology, Image resolution
Published
2006
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19. Crystal structure of a single-stranded DNA-binding protein (TM0604) from Thermotoga maritima at 2.60 Å resolution

Author

Glen Spraggon, Ian A. Wilson, Eileen Ambing, Ashley M. Deacon, Guenter Wolf, Jessica Paulsen, Peter Kuhn, Michael Hornsby, Edward Nigoghossian, Henry van den Bedem, Linda Okach, John Wooley, Joanna Hale, Raymond C. Stevens, Daniel McMullan, Tanya Biorac, Adam Godzik, Mark W. Knuth, Kevin Quijano, Scott A. Lesley, Kin Moy, Julie Feuerhelm, Heath E. Klock, Ron Reyes, Polat Abdubek, Eric Hampton, Eric Koesema, Hsiu-Ju Chiu, Slawomir K. Grzechnik, Keith O. Hodgson, Aprilfawn White, Jeff Velasquez, Christopher L. Rife, S. Sri Krishna, M.A. Elsliger, Carina Grittini, Mitchell D. Miller, Herbert L. Axelrod, Justin Haugen, Michael DiDonato, Andreas Kreusch, Robert Schwarzenbacher, Sanjay Agarwalla, Qingping Xu, and Lukasz Jaroszewski

Subjects
Models, Molecular, HMG-box, Molecular Sequence Data, DNA, Single-Stranded, Crystal structure, Crystallography, X-Ray, Biochemistry, DNA-binding protein, Protein Structure, Secondary, chemistry.chemical_compound, Plasmid, Protein structure, X-Ray Diffraction, Structural Biology, Escherichia coli, Thermotoga maritima, Amino Acid Sequence, Molecular Biology, Peptide sequence, biology, biology.organism_classification, Mitochondria, DNA-Binding Proteins, Crystallography, chemistry, Anisotropy, DNA, Plasmids, Transcription Factors
Published
2006
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20. Crystal structure of Hsp33 chaperone (TM1394) from Thermotoga maritima at 2.20 Å resolution

Author

Slawomir K. Grzechnik, Gye Won Han, Michael DiDonato, Heath E. Klock, Sanjay Agarwalla, John Wooley, Robert Schwarzenbacher, Daniel McMullan, Hsiu-Ju Chiu, Guenter Wolf, Ron Reyes, Marc-André Elsliger, Lukasz Jaroszewski, Polat Abdubek, Edward Nigoghossian, Raymond C. Stevens, Eric Hampton, Ashley M. Deacon, Tanya Biorac, Adam Godzik, Jaume M. Canaves, Qingping Xu, Ian A. Wilson, Jeff Velasquez, Mitchell D. Miller, Justin Haugen, Aprilfawn White, Eric Koesema, Kin Moy, Jessica Paulsen, Peter Kuhn, Eileen Ambing, Glen Spraggon, Juli Vincent, Kevin Quijano, Joanna Hale, Carina Grittini, Christopher L. Rife, Andreas Kreusch, Scott A. Lesley, Michael Hornsby, Henry van den Bedem, Herbert L. Axelrod, and Keith O. Hodgson

Subjects
biology, Chemistry, Molecular Sequence Data, Zinc Fingers, Crystal structure, biology.organism_classification, Biochemistry, Crystallography, Bacterial Proteins, Structural Biology, Thermotoga maritima, Chaperone (protein), Hsp33, biology.protein, Amino Acid Sequence, Crystallization, Molecular Biology, Heat-Shock Proteins, Molecular Chaperones
Published
2005
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21. Crystal structure of the global regulatory protein CsrA from Pseudomonas putida at 2.05 Å resolution reveals a new fold

Author

Keith O. Hodgson, Marc-André Elsliger, Edward Nigoghossian, Aprilfawn White, Lukasz Jaroszewski, Michael Hornsby, Henry van den Bedem, Guenter Wolf, Slawomir K. Grzechnik, Gye Won Han, Qingping Xu, Tanya Biorac, Adam Godzik, Kevin Quijano, Raymond C. Stevens, Joanna Hale, Hsiu-Ju Chiu, Herbert L. Axelrod, Heath E. Klock, Jessica Paulsen, Mitchell D. Miller, Scott A. Lesley, Carina Grittini, John Wooley, Christopher L. Rife, Robert Schwarzenbacher, Daniel McMullan, Michael DiDonato, Justin Haugen, Ron Reyes, Polat Abdubek, Jeff Velasquez, Eric Koesema, Juli Vincent, Eric Hampton, Peter Kuhn, Andreas Kreusch, Ian A. Wilson, Eileen Ambing, Kin Moy, Jaume M. Canaves, Ashley M. Deacon, Glen Spraggon, and Eric Sims

Subjects
Models, Molecular, Regulation of gene expression, Protein Folding, biology, Pseudomonas putida, Chemistry, Molecular Sequence Data, RNA-Binding Proteins, RNA-binding protein, Crystal structure, Crystallography, X-Ray, biology.organism_classification, Biochemistry, Microbiology, Bacterial Proteins, Structural Biology, Amino Acid Sequence, Dimerization, Molecular Biology
Published
2005
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22. Crystal structure of S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA) from Thermotoga maritima at 2.0 Å resolution reveals a new fold

Author

Polat Abdubek, Slawomir K. Grzechnik, Scott A. Lesley, Raymond C. Stevens, Kevin Quijano, Michael Hornsby, Henry van den Bedem, Guenter Wolf, Marc-André Elsliger, Heath E. Klock, Edward Nigoghossian, Lukasz Jaroszewski, Keith O. Hodgson, Jie Ouyang, John Wooley, Justin Haugen, Jaume M. Canaves, Jessica Paulsen, Aprilfawn White, Daniel McMullan, Inna Levin, Eric Koesema, Peter Kuhn, Ashley M. Deacon, Mitchell D. Miller, Gye Won Han, Qingping Xu, Ian A. Wilson, Herbert L. Axelrod, Hsiu-Ju Chiu, Eileen Ambing, Glen Spraggon, Tanya Biorac, Adam Godzik, Ron Reyes, Joanna Hale, Juli Vincent, Carina Grittini, Irimpan I. Mathews, Kin Moy, Andreas Kreusch, Michael DiDonato, Robert Schwarzenbacher, Eric Hampton, and Jeff Velasquez

Subjects
Models, Molecular, Protein Folding, biology, Protein Conformation, Chemistry, Stereochemistry, Crystal structure, Isomerase, Crystallography, X-Ray, Ligands, biology.organism_classification, Biochemistry, Protein structure, Structural Biology, Thermotoga maritima, Transfer RNA, Solvents, Protein folding, Isomerases, Molecular Biology
Published
2005
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23. Crystal structure of a novel manganese-containing cupin (TM1459) from Thermotoga maritima at 1.65 Å resolution

Author

Keith O. Hodgson, Raymond C. Stevens, Guenter Wolf, Kevin Quijano, Alyssa Robb, Andrew T. Morse, Juli Vincent, Heath E. Klock, Adam Godzik, Eric Koesema, Marc-André Elsliger, Andreas Kreusch, Rebecca Page, Frank von Delft, Timothy M. McPhillips, Inna Levin, Lukasz Jaroszewski, Jaume M. Canaves, Carina Grittini, Eric Sims, Xianhong Wang, Qingping Xu, Scott A. Lesley, Ashley M. Deacon, Linda S. Brinen, Jeff Velasquez, Ron Reyes, Slawomir K. Grzechnik, Ian A. Wilson, Kin Moy, Mike DiDonato, Jie Ouyang, Said Eshagi, Fred Rezezadeh, Henry van den Bedem, Glen Spraggon, John S. Kovarik, John Wooley, Xiaoping Dai, Daniel McMullan, Peter Kuhn, Bill West, Eric Hampton, Ross Floyd, Cathy Karlak, Mitchell D. Miller, and Robert Schwarzenbacher

Subjects
Models, Molecular, Molecular Sequence Data, chemistry.chemical_element, Crystal structure, Manganese, Biochemistry, Protein Structure, Secondary, Bacterial protein, Protein structure, Bacterial Proteins, Structural Biology, Thermotoga maritima, Amino Acid Sequence, Molecular Biology, Binding Sites, biology, Chemistry, Resolution (electron density), biology.organism_classification, Protein Structure, Tertiary, Structural homology, Crystallography, Structural Homology, Protein, Multiprotein Complexes, Crystallization, Oxidoreductases
Published
2004
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24. Crystal structure of a glycerophosphodiester phosphodiesterase (GDPD) from Thermotoga maritima (TM1621) at 1.60 Å resolution

Author

Slawomir K. Grzechnik, Henry van den Bedem, Bill West, Kevin Quijano, Guenter Wolf, Jamison Cambell, Eric Koesema, Heath E. Klock, Timothy M. McPhillips, Daniel McMullan, Kin Moy, Jaume M. Canaves, Andreas Kreusch, Rebecca Page, Eric Sims, Glen Spraggon, John Wooley, Fred Rezezadeh, John S. Kovarik, Marc-André Elsliger, Keith O. Hodgson, Alyssa Robb, Cathy Karlak, Xiaoping Dai, Jie Ouyang, Raymond C. Stevens, Andrew T. Morse, Juli Vincent, Frank von Delft, Said Eshagi, Eugenio Santelli, Carina Grittini, Xianhong Wang, Scott A. Lesley, Jeff Velasquez, Lukasz Jaroszewski, Robert Schwarzenbacher, Mitchell D. Miller, Qingping Xu, Ian A. Wilson, Ashley M. Deacon, Tanya Biorac, Adam Godzik, Linda S. Brinen, Peter Kuhn, and Ross Floyd

Subjects
Models, Molecular, Glycerophosphodiester phosphodiesterase, biology, Phosphoric Diester Hydrolases, Stereochemistry, Chemistry, Resolution (electron density), Reproducibility of Results, Phosphodiesterase, Crystal structure, Crystallography, X-Ray, biology.organism_classification, Biochemistry, Protein Structure, Secondary, Protein Structure, Tertiary, Structural Biology, Thermotoga maritima, Hydrolase, Crystallization, Molecular Biology
Published
2004
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25. Crystal structure of an HEPN domain protein (TM0613) from Thermotoga maritima at 1.75 Å resolution

Author

Adam Godzik, Jie Ouyang, Xiaoping Dai, Bill West, Timothy M. McPhillips, Daniel McMullan, John S. Kovarik, Mitchell D. Miller, Guenter Wolf, Andreas Kreusch, Keith O. Hodgson, Rebecca Page, Marc-André Elsliger, Kin Moy, Robert Schwarzenbacher, Frank von Delft, Henry van den Bedem, Linda S. Brinen, Heath E. Klock, Jeff Velasquez, Raymond C. Stevens, Lukasz Jaroszewski, Peter Kuhn, Jaume M. Canaves, Heidi Erlandsen, Ross Floyd, Eric Koesema, Alyssa Robb, Andrew T. Morse, Juli Vincent, Ashley M. Deacon, Glen Spraggon, Slawomir K. Grzechnik, Ian A. Wilson, Xianhong Wang, Scott A. Lesley, John Wooley, Carina Grittini, and Kevin Quijano

Subjects
Physics, biology, Protein domain, Resolution (electron density), Synchrotron radiation, Particle accelerator, Crystal structure, biology.organism_classification, Biochemistry, law.invention, Crystallography, Structural Biology, law, Chemical physics, Thermotoga maritima, Molecular Biology
Published
2004
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26. Crystal structure of uronate isomerase (TM0064) fromThermotoga maritimaat 2.85 Å resolution

Author

Keith O. Hodgson, Andreas Kreusch, Ian A. Wilson, Jie Ouyang, Henry van den Bedem, Lukasz Jaroszewski, Glen Spraggon, Xianhong Wang, Scott A. Lesley, Jaume M. Canaves, Chittibabu Guda, Alyssa Robb, Marc A. Elsliger, Bill West, Thomas L. Selby, Said Eshaghi, Raymond C. Stevens, Andrew T. Morse, Juli Vincent, Linda S. Brinen, Peter Kuhn, John S. Kovarik, Robert Schwarzenbacher, Ross Floyd, Adam Godzik, Daniel McMullan, John Wooley, Eric Koesema, Mitchell D. Miller, Jeff Velasquez, Ashley M. Deacon, Carina Grittini, Mark A. Miller, Slawomir K. Grzechnik, Kevin Rodrigues, Heath E. Klock, Xiaoping Dai, Kin Moy, Timothy M. McPhillips, Cathy Karlak, and Guenter Wolf

Subjects
Physics, Crystallography, biology, Structural Biology, Thermotoga maritima, Resolution (electron density), Crystal structure, Isomerase, biology.organism_classification, Molecular Biology, Biochemistry
Published
2003
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27. Crystal structure of thy1, a thymidylate synthase complementing protein fromThermotoga maritimaat 2.25 Å resolution

Author

Susan S. Taylor, Xiaoping Dai, Peter Kuhn, H. Klock, Eric Koesema, Ross Floyd, Ian A. Wilson, Irimpan I. Mathews, Jie Ouyang, Mark A. Miller, Kin Moy, Guenter Wolf, Lukasz Jaroszewski, Slawomir K. Grzechnik, Andreas Kreusch, Cathy Karlak, John M. Kovarik, Jeff Velasquez, Raymond C. Stevens, Alyssa Robb, Xianhong Wang, Scott A. Lesley, Timothy M. McPhillips, Linda S. Brinen, Carina Grittini, Ashley M. Deacon, Glen Spraggon, Andrew T. Morse, Juli Vincent, Mitchell D. Miller, Said Eshaghi, John Wooley, Jaume M. Canaves, Chittibabu Guda, Bill West, Thomas L. Selby, Kevin Rodrigues, Daniel McMullan, Adam Godzik, Henry van den Bedem, Keith O. Hodgson, and Marc A. Elsliger

Subjects
biology, Biochemistry, Structural Biology, Thermotoga maritima, Resolution (electron density), biology.protein, Crystal structure, biology.organism_classification, Molecular Biology, Thymidylate synthase
Published
2002
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28. Crystal structure of a putative quorum sensing-regulated protein (PA3611) from the Pseudomonas-specific DUF4146 family

Author

Das, Debanu, primary, Chiu, Hsiu-Ju, additional, Farr, Carol L., additional, Grant, Joanna C., additional, Jaroszewski, Lukasz, additional, Knuth, Mark W., additional, Miller, Mitchell D., additional, Tien, Henry J., additional, Elsliger, Marc-André, additional, Deacon, Ashley M., additional, Godzik, Adam, additional, Lesley, Scott A., additional, and Wilson, Ian A., additional

Published
2013
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29. Crystal structure of a member of a novel family of dioxygenases (PF10014) reveals a conserved cupin fold and active site

Author

Xu, Qingping, primary, Grant, Joanna, additional, Chiu, Hsiu-Ju, additional, Farr, Carol L., additional, Jaroszewski, Lukasz, additional, Knuth, Mark W., additional, Miller, Mitchell D., additional, Lesley, Scott A., additional, Godzik, Adam, additional, Elsliger, Marc-André, additional, Deacon, Ashley M., additional, and Wilson, Ian A., additional

Published
2013
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30. Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima

Author

Levisson, Mark, primary, Han, Gye Won, additional, Deller, Marc C., additional, Xu, Qingping, additional, Biely, Peter, additional, Hendriks, Sjon, additional, Ten Eyck, Lynn F., additional, Flensburg, Claus, additional, Roversi, Pietro, additional, Miller, Mitchell D., additional, McMullan, Daniel, additional, von Delft, Frank, additional, Kreusch, Andreas, additional, Deacon, Ashley M., additional, van der Oost, John, additional, Lesley, Scott A., additional, Elsliger, Marc-André, additional, Kengen, Servé W. M., additional, and Wilson, Ian A., additional

Published
2012
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31. Crystal structure of a metal‐dependent phosphoesterase (YP_910028.1) from Bifidobacterium adolescentis: Computational prediction and experimental validation of phosphoesterase activity

Author

Han, Gye Won, primary, Ko, Jaeju, additional, Farr, Carol L., additional, Deller, Marc C., additional, Xu, Qingping, additional, Chiu, Hsiu‐Ju, additional, Miller, Mitchell D., additional, Sefcikova, Jana, additional, Somarowthu, Srinivas, additional, Beuning, Penny J., additional, Elsliger, Marc‐André, additional, Deacon, Ashley M., additional, Godzik, Adam, additional, Lesley, Scott A., additional, Wilson, Ian A., additional, and Ondrechen, Mary Jo, additional

Published
2011
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33. Crystal structure of a novel Sm-like protein of putative cyanophage origin at 2.60 Å resolution

Author

Das, Debanu, primary, Kozbial, Piotr, additional, Axelrod, Herbert L., additional, Miller, Mitchell D., additional, McMullan, Daniel, additional, Krishna, S. Sri, additional, Abdubek, Polat, additional, Acosta, Claire, additional, Astakhova, Tamara, additional, Burra, Prasad, additional, Carlton, Dennis, additional, Chen, Connie, additional, Chiu, Hsiu-Ju, additional, Clayton, Thomas, additional, Deller, Marc C., additional, Duan, Lian, additional, Elias, Ylva, additional, Elsliger, Marc-André, additional, Ernst, Dustin, additional, Farr, Carol, additional, Feuerhelm, Julie, additional, Grzechnik, Anna, additional, Grzechnik, Slawomir K., additional, Hale, Joanna, additional, Han, Gye Won, additional, Jaroszewski, Lukasz, additional, Jin, Kevin K., additional, Johnson, Hope A., additional, Klock, Heath E., additional, Knuth, Mark W., additional, Kumar, Abhinav, additional, Marciano, David, additional, Morse, Andrew T., additional, Murphy, Kevin D., additional, Nigoghossian, Edward, additional, Nopakun, Amanda, additional, Okach, Linda, additional, Oommachen, Silvya, additional, Paulsen, Jessica, additional, Puckett, Christina, additional, Reyes, Ron, additional, Rife, Christopher L., additional, Sefcovic, Natasha, additional, Sudek, Sebastian, additional, Tien, Henry, additional, Trame, Christine, additional, Trout, Christina V., additional, van den Bedem, Henry, additional, Weekes, Dana, additional, White, Aprilfawn, additional, Xu, Qingping, additional, Hodgson, Keith O., additional, Wooley, John, additional, Deacon, Ashley M., additional, Godzik, Adam, additional, Lesley, Scott A., additional, and Wilson, Ian A., additional

Published
2008
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34. Crystal structure of the Fic (Filamentation induced by cAMP) family protein SO4266 (gi|24375750) from Shewanella oneidensis MR-1 at 1.6 Å resolution

Author

Das, Debanu, primary, Krishna, S. Sri, additional, McMullan, Daniel, additional, Miller, Mitchell D., additional, Xu, Qingping, additional, Abdubek, Polat, additional, Acosta, Claire, additional, Astakhova, Tamara, additional, Axelrod, Herbert L., additional, Burra, Prasad, additional, Carlton, Dennis, additional, Chiu, Hsiu-Ju, additional, Clayton, Thomas, additional, Deller, Marc C., additional, Duan, Lian, additional, Elias, Ylva, additional, Elsliger, Marc-André, additional, Ernst, Dustin, additional, Feuerhelm, Julie, additional, Grzechnik, Anna, additional, Grzechnik, Slawomir K., additional, Hale, Joanna, additional, Han, Gye Won, additional, Jaroszewski, Lukasz, additional, Jin, Kevin K., additional, Klock, Heath E., additional, Knuth, Mark W., additional, Kozbial, Piotr, additional, Kumar, Abhinav, additional, Marciano, David, additional, Morse, Andrew T., additional, Murphy, Kevin D., additional, Nigoghossian, Edward, additional, Okach, Linda, additional, Oommachen, Silvya, additional, Paulsen, Jessica, additional, Reyes, Ron, additional, Rife, Christopher L., additional, Sefcovic, Natasha, additional, Tien, Henry, additional, Trame, Christine B., additional, Trout, Christina V., additional, van den Bedem, Henry, additional, Weekes, Dana, additional, White, Aprilfawn, additional, Hodgson, Keith O., additional, Wooley, John, additional, Deacon, Ashley M., additional, Godzik, Adam, additional, Lesley, Scott A., additional, and Wilson, Ian A., additional

Published
2008
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35. Crystal structure of a novel archaeal AAA+ ATPase SSO1545 from Sulfolobus solfataricus

Author

Xu, Qingping, primary, Rife, Christopher L., additional, Carlton, Dennis, additional, Miller, Mitchell D., additional, Krishna, S. Sri, additional, Elsliger, Marc-André, additional, Abdubek, Polat, additional, Astakhova, Tamara, additional, Chiu, Hsiu-Ju, additional, Clayton, Thomas, additional, Duan, Lian, additional, Feuerhelm, Julie, additional, Grzechnik, Slawomir K., additional, Hale, Joanna, additional, Han, Gye Won, additional, Jaroszewski, Lukasz, additional, Jin, Kevin K., additional, Klock, Heath E., additional, Knuth, Mark W., additional, Kumar, Abhinav, additional, McMullan, Daniel, additional, Morse, Andrew T., additional, Nigoghossian, Edward, additional, Okach, Linda, additional, Oommachen, Silvya, additional, Paulsen, Jessica, additional, Reyes, Ron, additional, van den Bedem, Henry, additional, Hodgson, Keith O., additional, Wooley, John, additional, Deacon, Ashley M., additional, Godzik, Adam, additional, Lesley, Scott A., additional, and Wilson, Ian A., additional

Published
2008
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36. Crystal structures of MW1337R and lin2004: Representatives of a novel protein family that adopt a four‐helical bundle fold

Author

Kozbial, Piotr, primary, Xu, Qingping, additional, Chiu, Hsiu‐Ju, additional, McMullan, Daniel, additional, Krishna, S. Sri, additional, Miller, Mitchell D., additional, Abdubek, Polat, additional, Acosta, Claire, additional, Astakhova, Tamara, additional, Axelrod, Herbert L., additional, Carlton, Dennis, additional, Clayton, Thomas, additional, Deller, Marc, additional, Duan, Lian, additional, Elias, Ylva, additional, Elsliger, Marc‐André, additional, Feuerhelm, Julie, additional, Grzechnik, Slawomir K., additional, Hale, Joanna, additional, Han, Gye Won, additional, Jaroszewski, Lukasz, additional, Jin, Kevin K., additional, Klock, Heath E., additional, Knuth, Mark W., additional, Koesema, Eric, additional, Kumar, Abhinav, additional, Marciano, David, additional, Morse, Andrew T., additional, Murphy, Kevin D., additional, Nigoghossian, Edward, additional, Okach, Linda, additional, Oommachen, Silvya, additional, Reyes, Ron, additional, Rife, Christopher L., additional, Spraggon, Glen, additional, Trout, Christina V., additional, van den Bedem, Henry, additional, Weekes, Dana, additional, White, Aprilfawn, additional, Wolf, Guenter, additional, Zubieta, Chloe, additional, Hodgson, Keith O., additional, Wooley, John, additional, Deacon, Ashley M., additional, Godzik, Adam, additional, Lesley, Scott A., additional, and Wilson, Ian A., additional

Published
2008
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37. Crystal structure of an ADP-ribosylated protein with a cytidine deaminase-like fold, but unknown function (TM1506), from Thermotoga maritima at 2.70 Å resolution

Author

Xu, Qingping, primary, Kozbial, Piotr, additional, McMullan, Daniel, additional, Sri Krishna, S., additional, Brittain, Scott M., additional, Ficarro, Scott B., additional, DiDonato, Michael, additional, Miller, Mitchell D., additional, Abdubek, Polat, additional, Axelrod, Herbert L., additional, Chiu, Hsiu-Ju, additional, Clayton, Thomas, additional, Duan, Lian, additional, Elsliger, Marc-André, additional, Feuerhelm, Julie, additional, Grzechnik, Slawomir K., additional, Hale, Joanna, additional, Han, Gye Won, additional, Jaroszewski, Lukasz, additional, Klock, Heath E., additional, Morse, Andrew T., additional, Nigoghossian, Edward, additional, Paulsen, Jessica, additional, Reyes, Ron, additional, Rife, Christopher L., additional, van den Bedem, Henry, additional, White, Aprilfawn, additional, Hodgson, Keith O., additional, Wooley, John, additional, Deacon, Ashley M., additional, Godzik, Adam, additional, Lesley, Scott A., additional, and Wilson, Ian A., additional

Published
2008
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38. Crystal structure of AICAR transformylase IMP cyclohydrolase (TM1249) fromThermotoga maritima at 1.88 Å resolution

Author

Axelrod, Herbert L., primary, McMullan, Daniel, additional, Krishna, S. Sri, additional, Miller, Mitchell D., additional, Elsliger, Marc-Andre, additional, Abdubek, Polat, additional, Ambing, Eileen, additional, Astakhova, Tamara, additional, Carlton, Dennis, additional, Chiu, Hsiu-Ju, additional, Clayton, Thomas, additional, Duan, Lian, additional, Feuerhelm, Julie, additional, Grzechnik, Slawomir K., additional, Hale, Joanna, additional, Han, Gye Won, additional, Haugen, Justin, additional, Jaroszewski, Lukasz, additional, Jin, Kevin K., additional, Klock, Heath E., additional, Knuth, Mark W., additional, Koesema, Eric, additional, Morse, Andrew T., additional, Nigoghossian, Edward, additional, Okach, Linda, additional, Oommachen, Silvya, additional, Paulsen, Jessica, additional, Quijano, Kevin, additional, Reyes, Ron, additional, Rife, Christopher L., additional, van den Bedem, Henry, additional, Weekes, Dana, additional, White, Aprilfawn, additional, Wolf, Guenter, additional, Xu, Qingping, additional, Hodgson, Keith O., additional, Wooley, John, additional, Deacon, Ashley M., additional, Godzik, Adam, additional, Lesley, Scott A., additional, and Wilson, Ian A., additional

Published
2008
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39. Crystal structure of 2‐keto‐3‐deoxygluconate kinase (TM0067) from Thermotoga maritima at 2.05 Å resolution

Author

Mathews, Irimpan I., primary, McMullan, Daniel, additional, Miller, Mitchell D., additional, Canaves, Jaume M., additional, Elsliger, Marc‐André, additional, Floyd, Ross, additional, Grzechnik, Slawomir K., additional, Jaroszewski, Lukasz, additional, Klock, Heath E., additional, Koesema, Eric, additional, Kovarik, John S., additional, Kreusch, Andreas, additional, Kuhn, Peter, additional, McPhillips, Timothy M., additional, Morse, Andrew T., additional, Quijano, Kevin, additional, Rife, Christopher L., additional, Schwarzenbacher, Robert, additional, Spraggon, Glen, additional, Stevens, Raymond C., additional, van den Bedem, Henry, additional, Weekes, Dana, additional, Wolf, Guenter, additional, Hodgson, Keith O., additional, Wooley, John, additional, Deacon, Ashley M., additional, Godzik, Adam, additional, Lesley, Scott A., additional, and Wilson, Ian A., additional

Published
2007
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40. Crystal structures of two novel dye-decolorizing peroxidases reveal a β-barrel fold with a conserved heme-binding motif

Author

Zubieta, Chloe, primary, Krishna, S. Sri, additional, Kapoor, Mili, additional, Kozbial, Piotr, additional, McMullan, Daniel, additional, Axelrod, Herbert L., additional, Miller, Mitchell D., additional, Abdubek, Polat, additional, Ambing, Eileen, additional, Astakhova, Tamara, additional, Carlton, Dennis, additional, Chiu, Hsiu-Ju, additional, Clayton, Thomas, additional, Deller, Marc C., additional, Duan, Lian, additional, Elsliger, Marc-André, additional, Feuerhelm, Julie, additional, Grzechnik, Slawomir K., additional, Hale, Joanna, additional, Hampton, Eric, additional, Han, Gye Won, additional, Jaroszewski, Lukasz, additional, Jin, Kevin K., additional, Klock, Heath E., additional, Knuth, Mark W., additional, Kumar, Abhinav, additional, Marciano, David, additional, Morse, Andrew T., additional, Nigoghossian, Edward, additional, Okach, Linda, additional, Oommachen, Silvya, additional, Reyes, Ron, additional, Rife, Christopher L., additional, Schimmel, Paul, additional, Bedem, Henry van den, additional, Weekes, Dana, additional, White, Aprilfawn, additional, Xu, Qingping, additional, Hodgson, Keith O., additional, Wooley, John, additional, Deacon, Ashley M., additional, Godzik, Adam, additional, Lesley, Scott A., additional, and Wilson, Ian A., additional

Published
2007
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41. Crystal structure of MtnX phosphatase fromBacillus subtilisat 2.0 Å resolution provides a structural basis for bipartite phosphomonoester hydrolysis of 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate

Author

Xu, Qingping, primary, Saikatendu, Kumar Singh, additional, Krishna, S. Sri, additional, McMullan, Daniel, additional, Abdubek, Polat, additional, Agarwalla, Sanjay, additional, Ambing, Eileen, additional, Astakhova, Tamara, additional, Axelrod, Herbert L., additional, Carlton, Dennis, additional, Chiu, Hsiu-Ju, additional, Clayton, Thomas, additional, DiDonato, Michael, additional, Duan, Lian, additional, Elsliger, Marc-André, additional, Feuerhelm, Julie, additional, Grzechnik, Slawomir K., additional, Hale, Joanna, additional, Hampton, Eric, additional, Han, Gye Won, additional, Haugen, Justin, additional, Jaroszewski, Lukasz, additional, Jin, Kevin K., additional, Klock, Heath E., additional, Knuth, Mark W., additional, Koesema, Eric, additional, Miller, Mitchell D., additional, Morse, Andrew T., additional, Nigoghossian, Edward, additional, Okach, Linda, additional, Oommachen, Silvya, additional, Paulsen, Jessica, additional, Reyes, Ron, additional, Rife, Christopher L., additional, Schwarzenbacher, Robert, additional, van den Bedem, Henry, additional, White, Aprilfawn, additional, Wolf, Guenter, additional, Hodgson, Keith O., additional, Wooley, John, additional, Deacon, Ashley M., additional, Godzik, Adam, additional, Lesley, Scott A., additional, and Wilson, Ian A., additional

Published
2007
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42. Identification and structural characterization of heme binding in a novel dye‐decolorizing peroxidase, TyrA

Author

Zubieta, Chloe, primary, Joseph, Rosanne, additional, Sri Krishna, S., additional, McMullan, Daniel, additional, Kapoor, Mili, additional, Axelrod, Herbert L., additional, Miller, Mitchell D., additional, Abdubek, Polat, additional, Acosta, Claire, additional, Astakhova, Tamara, additional, Carlton, Dennis, additional, Chiu, Hsiu‐Ju, additional, Clayton, Thomas, additional, Deller, Marc C., additional, Duan, Lian, additional, Elias, Ylva, additional, Elsliger, Marc‐André, additional, Feuerhelm, Julie, additional, Grzechnik, Slawomir K., additional, Hale, Joanna, additional, Han, Gye Won, additional, Jaroszewski, Lukasz, additional, Jin, Kevin K., additional, Klock, Heath E., additional, Knuth, Mark W., additional, Kozbial, Piotr, additional, Kumar, Abhinav, additional, Marciano, David, additional, Morse, Andrew T., additional, Murphy, Kevin D., additional, Nigoghossian, Edward, additional, Okach, Linda, additional, Oommachen, Silvya, additional, Reyes, Ron, additional, Rife, Christopher L., additional, Schimmel, Paul, additional, Trout, Christina V., additional, van den Bedem, Henry, additional, Weekes, Dana, additional, White, Aprilfawn, additional, Xu, Qingping, additional, Hodgson, Keith O., additional, Wooley, John, additional, Deacon, Ashley M., additional, Godzik, Adam, additional, Lesley, Scott A., additional, and Wilson, Ian A., additional

Published
2007
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43. Crystal structure of NMA1982 from Neisseria meningitidis at 1.5 Å resolution provides a structural scaffold for nonclassical, eukaryotic‐like phosphatases

Author

Krishna, S. Sri, primary, Tautz, Lutz, additional, Xu, Qingping, additional, McMullan, Daniel, additional, Miller, Mitchell D., additional, Abdubek, Polat, additional, Ambing, Eileen, additional, Astakhova, Tamara, additional, Axelrod, Herbert L., additional, Carlton, Dennis, additional, Chiu, Hsiu‐Ju, additional, Clayton, Thomas, additional, DiDonato, Michael, additional, Duan, Lian, additional, Elsliger, Marc‐André, additional, Grzechnik, Slawomir K., additional, Hale, Joanna, additional, Hampton, Eric, additional, Han, Gye Won, additional, Haugen, Justin, additional, Jaroszewski, Lukasz, additional, Jin, Kevin K., additional, Klock, Heath E., additional, Knuth, Mark W., additional, Koesema, Eric, additional, Morse, Andrew T., additional, Mustelin, Tomas, additional, Nigoghossian, Edward, additional, Oommachen, Silvya, additional, Reyes, Ron, additional, Rife, Christopher L., additional, Bedem, Henry van den, additional, Weekes, Dana, additional, White, Aprilfawn, additional, Hodgson, Keith O., additional, Wooley, John, additional, Deacon, Ashley M., additional, Godzik, Adam, additional, Lesley, Scott A., additional, and Wilson, Ian A., additional

Published
2007
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44. Crystal structure of homoserine O‐succinyltransferase from Bacillus cereus at 2.4 Å resolution

Author

Zubieta, Chloe, primary, Krishna, S. Sri, additional, McMullan, Daniel, additional, Miller, Mitchell D., additional, Abdubek, Polat, additional, Agarwalla, Sanjay, additional, Ambing, Eileen, additional, Astakhova, Tamara, additional, Axelrod, Herbert L., additional, Carlton, Dennis, additional, Chiu, Hsiu‐Ju, additional, Clayton, Thomas, additional, Deller, Marc, additional, DiDonato, Michael, additional, Duan, Lian, additional, Elsliger, Marc‐André, additional, Grzechnik, Slawomir K., additional, Hale, Joanna, additional, Hampton, Eric, additional, Han, Gye Won, additional, Haugen, Justin, additional, Jaroszewski, Lukasz, additional, Jin, Kevin K., additional, Klock, Heath E., additional, Knuth, Mark W., additional, Koesema, Eric, additional, Kumar, Abhinav, additional, Marciano, David, additional, Morse, Andrew T., additional, Nigoghossian, Edward, additional, Oommachen, Silvya, additional, Reyes, Ron, additional, Rife, Christopher L., additional, Bedem, Henry van den, additional, Weekes, Dana, additional, White, Aprilfawn, additional, Xu, Qingping, additional, Hodgson, Keith O., additional, Wooley, John, additional, Deacon, Ashley M., additional, Godzik, Adam, additional, Lesley, Scott A., additional, and Wilson, Ian A., additional

Published
2007
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45. Crystal structure of TM1030 from Thermotoga maritima at 2.3 Å resolution reveals molecular details of its transcription repressor function

Author

Premkumar, Lakshmanane, primary, Rife, Christopher L., additional, Sri Krishna, S., additional, McMullan, Daniel, additional, Miller, Mitchell D., additional, Abdubek, Polat, additional, Ambing, Eileen, additional, Astakhova, Tamara, additional, Axelrod, Herbert L., additional, Canaves, Jaume M., additional, Carlton, Dennis, additional, Chiu, Hsiu-Ju, additional, Clayton, Thomas, additional, DiDonato, Michael, additional, Duan, Lian, additional, Elsliger, Marc-André, additional, Feuerhelm, Julie, additional, Floyd, Ross, additional, Grzechnik, Slawomir K., additional, Hale, Joanna, additional, Hampton, Eric, additional, Han, Gye Won, additional, Haugen, Justin, additional, Jaroszewski, Lukasz, additional, Jin, Kevin K., additional, Klock, Heath E., additional, Knuth, Mark W., additional, Koesema, Eric, additional, Kovarik, John S., additional, Kreusch, Andreas, additional, Levin, Inna, additional, McPhillips, Timothy M., additional, Morse, Andrew T., additional, Nigoghossian, Edward, additional, Okach, Linda, additional, Oommachen, Silvya, additional, Paulsen, Jessica, additional, Quijano, Kevin, additional, Reyes, Ron, additional, Rezezadeh, Fred, additional, Rodionov, Dmitry, additional, Schwarzenbacher, Robert, additional, Spraggon, Glen, additional, van den Bedem, Henry, additional, White, Aprilfawn, additional, Wolf, Guenter, additional, Xu, Qingping, additional, Hodgson, Keith O., additional, Wooley, John, additional, Deacon, Ashley M., additional, Godzik, Adam, additional, Lesley, Scott A., additional, and Wilson, Ian A., additional

Published
2007
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46. Crystal structure of a transcription regulator (TM1602) from Thermotoga maritima at 2.3 Å resolution

Author

Weekes, Dana, primary, Miller, Mitchell D., additional, Krishna, S. Sri, additional, McMullan, Daniel, additional, McPhillips, Timothy M., additional, Acosta, Claire, additional, Canaves, Jaume M., additional, Elsliger, Marc-André, additional, Floyd, Ross, additional, Grzechnik, Slawomir K., additional, Jaroszewski, Lukasz, additional, Klock, Heath E., additional, Koesema, Eric, additional, Kovarik, John S., additional, Kreusch, Andreas, additional, Morse, Andrew T., additional, Quijano, Kevin, additional, Spraggon, Glen, additional, van den Bedem, Henry, additional, Wolf, Guenter, additional, Hodgson, Keith O., additional, Wooley, John, additional, Deacon, Ashley M., additional, Godzik, Adam, additional, Lesley, Scott A., additional, and Wilson, Ian A., additional

Published
2007
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47. Crystal structure of an ORFan protein (TM1622) fromThermotoga maritimaat 1.75 Å resolution reveals a fold similar to the Ran-binding protein Mog1p

Author

Xu, Qingping, primary, Krishna, S. Sri, additional, McMullan, Daniel, additional, Schwarzenbacher, Robert, additional, Miller, Mitchell D., additional, Abdubek, Polat, additional, Agarwalla, Sanjay, additional, Ambing, Eileen, additional, Astakhova, Tamara, additional, Axelrod, Herbert L., additional, Canaves, Jaume M., additional, Carlton, Dennis, additional, Chiu, Hsiu-Ju, additional, Clayton, Thomas, additional, DiDonato, Michael, additional, Duan, Lian, additional, Elsliger, Marc-André, additional, Feuerhelm, Julie, additional, Grzechnik, Slawomir K., additional, Hale, Joanna, additional, Hampton, Eric, additional, Han, Gye Won, additional, Haugen, Justin, additional, Jaroszewski, Lukasz, additional, Jin, Kevin K., additional, Klock, Heath E., additional, Knuth, Mark W., additional, Koesema, Eric, additional, Kreusch, Andreas, additional, Kuhn, Peter, additional, Morse, Andrew T., additional, Nigoghossian, Edward, additional, Okach, Linda, additional, Oommachen, Silvya, additional, Paulsen, Jessica, additional, Quijano, Kevin, additional, Reyes, Ron, additional, Rife, Christopher L., additional, Spraggon, Glen, additional, Stevens, Raymond C., additional, van den Bedem, Henry, additional, White, Aprilfawn, additional, Wolf, Guenter, additional, Hodgson, Keith O., additional, Wooley, John, additional, Deacon, Ashley M., additional, Godzik, Adam, additional, Lesley, Scott A., additional, and Wilson, Ian A., additional

Published
2006
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48. Crystal structure of 2-phosphosulfolactate phosphatase (ComB) fromClostridium acetobutylicumat 2.6 Å resolution reveals a new fold with a novel active site

Author

DiDonato, Michael, primary, Krishna, S. Sri, additional, Schwarzenbacher, Robert, additional, McMullan, Daniel, additional, Agarwalla, Sanjay, additional, Brittain, Scott M., additional, Miller, Mitchell D., additional, Abdubek, Polat, additional, Ambing, Eileen, additional, Axelrod, Herbert L., additional, Canaves, Jaume M., additional, Chiu, Hsiu-Ju, additional, Deacon, Ashley M., additional, Duan, Lian, additional, Elsliger, Marc-André, additional, Godzik, Adam, additional, Grzechnik, Slawomir K., additional, Hale, Joanna, additional, Hampton, Eric, additional, Haugen, Justin, additional, Jaroszewski, Lukasz, additional, Jin, Kevin K., additional, Klock, Heath E., additional, Knuth, Mark W., additional, Koesema, Eric, additional, Kreusch, Andreas, additional, Kuhn, Peter, additional, Lesley, Scott A., additional, Levin, Inna, additional, Morse, Andrew T., additional, Nigoghossian, Edward, additional, Okach, Linda, additional, Oommachen, Silvya, additional, Paulsen, Jessica, additional, Quijano, Kevin, additional, Reyes, Ron, additional, Rife, Christopher L., additional, Spraggon, Glen, additional, Stevens, Raymond C., additional, van den Bedem, Henry, additional, White, Aprilfawn, additional, Wolf, Guenter, additional, Xu, Qingping, additional, Hodgson, Keith O., additional, Wooley, John, additional, and Wilson, Ian A., additional

Published
2006
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49. Comparative structural analysis of a novel glutathioneS-transferase (ATU5508) fromAgrobacterium tumefaciensat 2.0 Å resolution

Author

Kosloff, Mickey, primary, Han, Gye Won, additional, Krishna, S. Sri, additional, Schwarzenbacher, Robert, additional, Fasnacht, Marc, additional, Elsliger, Marc-André, additional, Abdubek, Polat, additional, Agarwalla, Sanjay, additional, Ambing, Eileen, additional, Astakhova, Tamara, additional, Axelrod, Herbert L., additional, Canaves, Jaume M., additional, Carlton, Dennis, additional, Chiu, Hsiu-Ju, additional, Clayton, Thomas, additional, DiDonato, Michael, additional, Duan, Lian, additional, Feuerhelm, Julie, additional, Grittini, Carina, additional, Grzechnik, Slawomir K., additional, Hale, Joanna, additional, Hampton, Eric, additional, Haugen, Justin, additional, Jaroszewski, Lukasz, additional, Jin, Kevin K., additional, Johnson, Hope, additional, Klock, Heath E., additional, Knuth, Mark W., additional, Koesema, Eric, additional, Kreusch, Andreas, additional, Kuhn, Peter, additional, Levin, Inna, additional, McMullan, Daniel, additional, Miller, Mitchell D., additional, Morse, Andrew T., additional, Moy, Kin, additional, Nigoghossian, Edward, additional, Okach, Linda, additional, Oommachen, Silvya, additional, Page, Rebecca, additional, Paulsen, Jessica, additional, Quijano, Kevin, additional, Reyes, Ron, additional, Rife, Christopher L., additional, Sims, Eric, additional, Spraggon, Glen, additional, Sridhar, Vandana, additional, Stevens, Raymond C., additional, van den Bedem, Henry, additional, Velasquez, Jeff, additional, White, Aprilfawn, additional, Wolf, Guenter, additional, Xu, Qingping, additional, Hodgson, Keith O., additional, Wooley, John, additional, Deacon, Ashley M., additional, Godzik, Adam, additional, Lesley, Scott A., additional, and Wilson, Ian A., additional

Published
2006
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50. Crystal structure of a glycerate kinase (TM1585) from Thermotoga maritima at 2.70 Å resolution reveals a new fold

Author

Schwarzenbacher, Robert, primary, McMullan, Daniel, additional, Krishna, S. Sri, additional, Xu, Qingping, additional, Miller, Mitchell D., additional, Canaves, Jaume M., additional, Elsliger, Marc-André, additional, Floyd, Ross, additional, Grzechnik, Slawomir K., additional, Jaroszewski, Lukasz, additional, Klock, Heath E., additional, Koesema, Eric, additional, Kovarik, John S., additional, Kreusch, Andreas, additional, Kuhn, Peter, additional, McPhillips, Timothy M., additional, Morse, Andrew T., additional, Quijano, Kevin, additional, Spraggon, Glen, additional, Stevens, Raymond C., additional, van den Bedem, Henry, additional, Wolf, Guenter, additional, Hodgson, Keith O., additional, Wooley, John, additional, Deacon, Ashley M., additional, Godzik, Adam, additional, Lesley, Scott A., additional, and Wilson, Ian A., additional

Published
2006
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