Search

Your search keyword '"Ambing E"' showing total 42 results
Start Over Author "Ambing E"
42 results on '"Ambing E"'

1. NRX-0492 degrades wild-type and C481 mutant BTK and demonstrates in vivo activity in CLL patient-derived xenografts.

Author

Zhang D, Harris HM, Chen J, Judy J, James G, Kelly A, McIntosh J, Tenn-McClellan A, Ambing E, Tan YS, Lu H, Gajewski S, Clifton MC, Yung S, Robbins DW, Pirooznia M, Skånland SS, Gaglione E, Mhibik M, Underbayev C, Ahn IE, Sun C, Herman SEM, Noviski M, and Wiestner A

Subjects
Humans, Agammaglobulinaemia Tyrosine Kinase, Heterografts, Drug Resistance, Neoplasm, Protein Kinase Inhibitors pharmacology, Protein Kinase Inhibitors therapeutic use, Pyrimidines therapeutic use, Leukemia, Lymphocytic, Chronic, B-Cell drug therapy, Leukemia, Lymphocytic, Chronic, B-Cell genetics, Leukemia, Lymphocytic, Chronic, B-Cell metabolism
Abstract

Bruton tyrosine kinase (BTK) is essential for B-cell receptor (BCR) signaling, a driver of chronic lymphocytic leukemia (CLL). Covalent inhibitors bind C481 in the active site of BTK and have become a preferred CLL therapy. Disease progression on covalent BTK inhibitors is commonly associated with C481 mutations. Here, we investigated a targeted protein degrader, NRX-0492, that links a noncovalent BTK-binding domain to cereblon, an adaptor protein of the E3 ubiquitin ligase complex. NRX-0492 selectively catalyzes ubiquitylation and proteasomal degradation of BTK. In primary CLL cells, NRX-0492 induced rapid and sustained degradation of both wild-type and C481 mutant BTK at half maximal degradation concentration (DC50) of ≤0.2 nM and DC90 of ≤0.5 nM, respectively. Sustained degrader activity was maintained for at least 24 hours after washout and was equally observed in high-risk (deletion 17p) and standard-risk (deletion 13q only) CLL subtypes. In in vitro testing against treatment-naïve CLL samples, NRX-0492 was as effective as ibrutinib at inhibiting BCR-mediated signaling, transcriptional programs, and chemokine secretion. In patient-derived xenografts, orally administered NRX-0492 induced BTK degradation and inhibited activation and proliferation of CLL cells in blood and spleen and remained efficacious against primary C481S mutant CLL cells collected from a patient progressing on ibrutinib. Oral bioavailability, >90% degradation of BTK at subnanomolar concentrations, and sustained pharmacodynamic effects after drug clearance make this class of targeted protein degraders uniquely suitable for clinical translation, in particular as a strategy to overcome BTK inhibitor resistance. Clinical studies testing this approach have been initiated (NCT04830137, NCT05131022).

Published
2023
Full Text
View/download PDF

2. The structural mechanism of human glycogen synthesis by the GYS1-GYG1 complex.

Author

Fastman NM, Liu Y, Ramanan V, Merritt H, Ambing E, DePaoli-Roach AA, Roach PJ, Hurley TD, Mellem KT, Ullman JC, Green E, Morgans D Jr, and Tzitzilonis C

Subjects
Glucosyltransferases metabolism, Glycogen metabolism, Humans, Glycogen Synthase metabolism, Glycogenolysis, Glycoproteins metabolism
Abstract

Glycogen is the primary energy reserve in mammals, and dysregulation of glycogen metabolism can result in glycogen storage diseases (GSDs). In muscle, glycogen synthesis is initiated by the enzymes glycogenin-1 (GYG1), which seeds the molecule by autoglucosylation, and glycogen synthase-1 (GYS1), which extends the glycogen chain. Although both enzymes are required for proper glycogen production, the nature of their interaction has been enigmatic. Here, we present the human GYS1:GYG1 complex in multiple conformations representing different functional states. We observe an asymmetric conformation of GYS1 that exposes an interface for close GYG1 association, and propose this state facilitates handoff of the GYG1-associated glycogen chain to a GYS1 subunit for elongation. Full activation of GYS1 widens the GYG1-binding groove, enabling GYG1 release concomitant with glycogen chain growth. This structural mechanism connecting chain nucleation and extension explains the apparent stepwise nature of glycogen synthesis and suggests distinct states to target for GSD-modifying therapeutics., Competing Interests: Declaration of interests N.M.F., Y.L., H.M., E.A., K.T.M., J.C.U., E.G., D.M., and C.T. are full time employees and stockholders of Maze Therapeutics. V.R., A.D.-R., and T.D.H. are advisors and stockholders of Maze Therapeutics., (Copyright © 2022 The Author(s). Published by Elsevier Inc. All rights reserved.)

Published
2022
Full Text
View/download PDF

3. Structure of a tryptophanyl-tRNA synthetase containing an iron-sulfur cluster.

Author

Han GW, Yang XL, McMullan D, Chong YE, Krishna SS, Rife CL, Weekes D, Brittain SM, Abdubek P, Ambing E, Astakhova T, Axelrod HL, Carlton D, Caruthers J, Chiu HJ, Clayton T, Duan L, Feuerhelm J, Grant JC, Grzechnik SK, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kumar A, Marciano D, Miller MD, Morse AT, Nigoghossian E, Okach L, Paulsen J, Reyes R, van den Bedem H, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, Elsliger MA, Schimmel P, and Wilson IA

Subjects
Amino Acid Sequence, Animals, Conserved Sequence, Crystallography, X-Ray, Humans, Ligands, Models, Molecular, Molecular Sequence Data, Protein Structure, Quaternary, Protein Structure, Tertiary, Sequence Alignment, Iron-Sulfur Proteins chemistry, Thermotoga maritima enzymology, Tryptophan-tRNA Ligase chemistry
Abstract

A novel aminoacyl-tRNA synthetase that contains an iron-sulfur cluster in the tRNA anticodon-binding region and efficiently charges tRNA with tryptophan has been found in Thermotoga maritima. The crystal structure of TmTrpRS (tryptophanyl-tRNA synthetase; TrpRS; EC 6.1.1.2) reveals an iron-sulfur [4Fe-4S] cluster bound to the tRNA anticodon-binding (TAB) domain and an L-tryptophan ligand in the active site. None of the other T. maritima aminoacyl-tRNA synthetases (AARSs) contain this [4Fe-4S] cluster-binding motif (C-x₂₂-C-x₆-C-x₂-C). It is speculated that the iron-sulfur cluster contributes to the stability of TmTrpRS and could play a role in the recognition of the anticodon.

Published
2010
Full Text
View/download PDF

4. Crystal structure of the ALK (anaplastic lymphoma kinase) catalytic domain.

Author

Lee CC, Jia Y, Li N, Sun X, Ng K, Ambing E, Gao MY, Hua S, Chen C, Kim S, Michellys PY, Lesley SA, Harris JL, and Spraggon G

Subjects
Adenosine Diphosphate chemistry, Adenosine Diphosphate metabolism, Amino Acid Motifs genetics, Amino Acid Sequence, Anaplastic Lymphoma Kinase, Animals, Cell Line, Crystallization, Crystallography, X-Ray, Humans, Kinetics, Models, Molecular, Molecular Sequence Data, Mutagenesis, Mutant Proteins metabolism, Neuroblastoma enzymology, Neuroblastoma genetics, Phosphorylation, Protein Binding, Protein-Tyrosine Kinases genetics, Protein-Tyrosine Kinases metabolism, Receptor Protein-Tyrosine Kinases, Sequence Homology, Amino Acid, Spodoptera, Staurosporine chemistry, Staurosporine metabolism, Substrate Specificity, Catalytic Domain, Mutant Proteins chemistry, Protein Conformation, Protein-Tyrosine Kinases chemistry
Abstract

ALK (anaplastic lymphoma kinase) is an RTK (receptor tyrosine kinase) of the IRK (insulin receptor kinase) superfamily, which share an YXXXYY autophosphorylation motif within their A-loops (activation loops). A common activation and regulatory mechanism is believed to exist for members of this superfamily typified by IRK and IGF1RK (insulin-like growth factor receptor kinase-1). Chromosomal translocations involving ALK were first identified in anaplastic large-cell lymphoma, a subtype of non-Hodgkin's lymphoma, where aberrant fusion of the ALK kinase domain with the NPM (nucleophosmin) dimerization domain results in autophosphosphorylation and ligand-independent activation. Activating mutations within the full-length ALK kinase domain, most commonly R1275Q and F1174L, which play a major role in neuroblastoma, were recently identified. To provide a structural framework for understanding these mutations and to guide structure-assisted drug discovery efforts, the X-ray crystal structure of the unphosphorylated ALK catalytic domain was determined in the apo, ADP- and staurosporine-bound forms. The structures reveal a partially inactive protein kinase conformation distinct from, and lacking, many of the negative regulatory features observed in inactive IGF1RK/IRK structures in their unphosphorylated forms. The A-loop adopts an inhibitory pose where a short proximal A-loop helix (alphaAL) packs against the alphaC helix and a novel N-terminal beta-turn motif, whereas the distal portion obstructs part of the predicted peptide-binding region. The structure helps explain the reported unique peptide substrate specificity and the importance of phosphorylation of the first A-loop Tyr1278 for kinase activity and NPM-ALK transforming potential. A single amino acid difference in the ALK substrate peptide binding P-1 site (where the P-site is the phosphoacceptor site) was identified that, in conjunction with A-loop sequence variation including the RAS (Arg-Ala-Ser)-motif, rationalizes the difference in the A-loop tyrosine autophosphorylation preference between ALK and IGF1RK/IRK. Enzymatic analysis of recombinant R1275Q and F1174L ALK mutant catalytic domains confirms the enhanced activity and transforming potential of these mutants. The transforming ability of the full-length ALK mutants in soft agar colony growth assays corroborates these findings. The availability of a three-dimensional structure for ALK will facilitate future structure-function and rational drug design efforts targeting this receptor tyrosine kinase.

Published
2010
Full Text
View/download PDF

5. Structural basis of murein peptide specificity of a gamma-D-glutamyl-l-diamino acid endopeptidase.

Author

Xu Q, Sudek S, McMullan D, Miller MD, Geierstanger B, Jones DH, Krishna SS, Spraggon G, Bursalay B, Abdubek P, Acosta C, Ambing E, Astakhova T, Axelrod HL, Carlton D, Caruthers J, Chiu HJ, Clayton T, Deller MC, Duan L, Elias Y, Elsliger MA, Feuerhelm J, Grzechnik SK, Hale J, Han GW, Haugen J, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kozbial P, Kumar A, Marciano D, Morse AT, Nigoghossian E, Okach L, Oommachen S, Paulsen J, Reyes R, Rife CL, Trout CV, van den Bedem H, Weekes D, White A, Wolf G, Zubieta C, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, and Wilson IA

Subjects
Amino Acid Sequence, Anabaena variabilis chemistry, Anabaena variabilis enzymology, Catalytic Domain, Cysteine Endopeptidases chemistry, Cysteine Endopeptidases metabolism, Cysteine Endopeptidases physiology, Endopeptidases physiology, Models, Biological, Models, Molecular, Molecular Sequence Data, Nostoc chemistry, Nostoc enzymology, Peptide Fragments chemistry, Peptide Fragments metabolism, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Substrate Specificity, src Homology Domains, Endopeptidases chemistry, Endopeptidases metabolism, Peptidoglycan chemistry, Peptidoglycan metabolism
Abstract

The crystal structures of two homologous endopeptidases from cyanobacteria Anabaena variabilis and Nostoc punctiforme were determined at 1.05 and 1.60 A resolution, respectively, and contain a bacterial SH3-like domain (SH3b) and a ubiquitous cell-wall-associated NlpC/P60 (or CHAP) cysteine peptidase domain. The NlpC/P60 domain is a primitive, papain-like peptidase in the CA clan of cysteine peptidases with a Cys126/His176/His188 catalytic triad and a conserved catalytic core. We deduced from structure and sequence analysis, and then experimentally, that these two proteins act as gamma-D-glutamyl-L-diamino acid endopeptidases (EC 3.4.22.-). The active site is located near the interface between the SH3b and NlpC/P60 domains, where the SH3b domain may help define substrate specificity, instead of functioning as a targeting domain, so that only muropeptides with an N-terminal L-alanine can bind to the active site.

Published
2009
Full Text
View/download PDF

6. Crystal structure of AICAR transformylase IMP cyclohydrolase (TM1249) from Thermotoga maritima at 1.88 A resolution.

Author

Axelrod HL, McMullan D, Krishna SS, Miller MD, Elsliger MA, Abdubek P, Ambing E, Astakhova T, Carlton D, Chiu HJ, Clayton T, Duan L, Feuerhelm J, Grzechnik SK, Hale J, Han GW, Haugen J, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Koesema E, Morse AT, Nigoghossian E, Okach L, Oommachen S, Paulsen J, Quijano K, Reyes R, Rife CL, van den Bedem H, Weekes D, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, and Wilson IA

Subjects
Amino Acid Sequence, Binding Sites, Crystallization, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Thermotoga maritima enzymology, Hydroxymethyl and Formyl Transferases chemistry, Multienzyme Complexes chemistry, Nucleotide Deaminases chemistry
Published
2008
Full Text
View/download PDF

7. Crystal structures of two novel dye-decolorizing peroxidases reveal a beta-barrel fold with a conserved heme-binding motif.

Author

Zubieta C, Krishna SS, Kapoor M, Kozbial P, McMullan D, Axelrod HL, Miller MD, Abdubek P, Ambing E, Astakhova T, Carlton D, Chiu HJ, Clayton T, Deller MC, Duan L, Elsliger MA, Feuerhelm J, Grzechnik SK, Hale J, Hampton E, Han GW, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kumar A, Marciano D, Morse AT, Nigoghossian E, Okach L, Oommachen S, Reyes R, Rife CL, Schimmel P, van den Bedem H, Weekes D, White A, Xu Q, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, and Wilson IA

Subjects
Amino Acid Motifs, Amino Acid Sequence, Bacterial Proteins physiology, Bacteroides enzymology, Catalytic Domain, Crystallography, X-Ray, Molecular Sequence Data, Multienzyme Complexes physiology, Peroxidases metabolism, Protein Binding, Protein Structure, Secondary, Shewanella enzymology, Bacterial Proteins chemistry, Coloring Agents metabolism, Conserved Sequence, Heme metabolism, Multienzyme Complexes chemistry, Peroxidases chemistry, Protein Folding
Abstract

BtDyP from Bacteroides thetaiotaomicron (strain VPI-5482) and TyrA from Shewanella oneidensis are dye-decolorizing peroxidases (DyPs), members of a new family of heme-dependent peroxidases recently identified in fungi and bacteria. Here, we report the crystal structures of BtDyP and TyrA at 1.6 and 2.7 A, respectively. BtDyP assembles into a hexamer, while TyrA assembles into a dimer; the dimerization interface is conserved between the two proteins. Each monomer exhibits a two-domain, alpha+beta ferredoxin-like fold. A site for heme binding was identified computationally, and modeling of a heme into the proposed active site allowed for identification of residues likely to be functionally important. Structural and sequence comparisons with other DyPs demonstrate a conservation of putative heme-binding residues, including an absolutely conserved histidine. Isothermal titration calorimetry experiments confirm heme binding, but with a stoichiometry of 0.3:1 (heme:protein)., ((c) 2007 Wiley-Liss, Inc.)

Published
2007
Full Text
View/download PDF

8. Crystal structure of MtnX phosphatase from Bacillus subtilis at 2.0 angstroms resolution provides a structural basis for bipartite phosphomonoester hydrolysis of 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate.

Author

Xu Q, Saikatendu KS, Krishna SS, McMullan D, Abdubek P, Agarwalla S, Ambing E, Astakhova T, Axelrod HL, Carlton D, Chiu HJ, Clayton T, DiDonato M, Duan L, Elsliger MA, Feuerhelm J, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Koesema E, Miller MD, Morse AT, Nigoghossian E, Okach L, Oommachen S, Paulsen J, Reyes R, Rife CL, Schwarzenbacher R, van den Bedem H, White A, Wolf G, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, and Wilson IA

Subjects
Amino Acid Sequence, Bacterial Proteins chemistry, Bacterial Proteins physiology, Crystallography, X-Ray, Hydrolysis, Molecular Sequence Data, Organophosphates chemistry, Thioglycosides chemistry, Bacillus subtilis enzymology, Organophosphates metabolism, Phosphoric Monoester Hydrolases chemistry, Phosphoric Monoester Hydrolases physiology, Thioglycosides metabolism
Published
2007
Full Text
View/download PDF

9. Crystal structure of NMA1982 from Neisseria meningitidis at 1.5 angstroms resolution provides a structural scaffold for nonclassical, eukaryotic-like phosphatases.

Author

Krishna SS, Tautz L, Xu Q, McMullan D, Miller MD, Abdubek P, Ambing E, Astakhova T, Axelrod HL, Carlton D, Chiu HJ, Clayton T, DiDonato M, Duan L, Elsliger MA, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Koesema E, Morse AT, Mustelin T, Nigoghossian E, Oommachen S, Reyes R, Rife CL, van den Bedem H, Weekes D, White A, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, and Wilson IA

Subjects
Amino Acid Motifs, Amino Acid Sequence, Bacterial Proteins metabolism, Bacterial Proteins physiology, Binding Sites, Crystallography, X-Ray, Molecular Sequence Data, Phosphoric Monoester Hydrolases metabolism, Phosphoric Monoester Hydrolases physiology, Protein Structure, Secondary, Bacterial Proteins chemistry, Neisseria meningitidis enzymology, Phosphoric Monoester Hydrolases chemistry
Published
2007
Full Text
View/download PDF

10. Crystal structure of homoserine O-succinyltransferase from Bacillus cereus at 2.4 A resolution.

Author

Zubieta C, Krishna SS, McMullan D, Miller MD, Abdubek P, Agarwalla S, Ambing E, Astakhova T, Axelrod HL, Carlton D, Chiu HJ, Clayton T, Deller M, DiDonato M, Duan L, Elsliger MA, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Koesema E, Kumar A, Marciano D, Morse AT, Nigoghossian E, Oommachen S, Reyes R, Rife CL, van den Bedem H, Weekes D, White A, Xu Q, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, and Wilson IA

Subjects
Amino Acid Sequence, Bacterial Proteins chemistry, Crystallography, X-Ray, Dimerization, Haemophilus influenzae enzymology, Models, Molecular, Molecular Sequence Data, Protein Conformation, Bacillus cereus enzymology, Homoserine O-Succinyltransferase chemistry
Published
2007
Full Text
View/download PDF

11. Crystal structure of TM1030 from Thermotoga maritima at 2.3 A resolution reveals molecular details of its transcription repressor function.

Author

Premkumar L, Rife CL, Sri Krishna S, McMullan D, Miller MD, Abdubek P, Ambing E, Astakhova T, Axelrod HL, Canaves JM, Carlton D, Chiu HJ, Clayton T, DiDonato M, Duan L, Elsliger MA, Feuerhelm J, Floyd R, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Koesema E, Kovarik JS, Kreusch A, Levin I, McPhillips TM, Morse AT, Nigoghossian E, Okach L, Oommachen S, Paulsen J, Quijano K, Reyes R, Rezezadeh F, Rodionov D, Schwarzenbacher R, Spraggon G, van den Bedem H, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, and Wilson IA

Subjects
Amino Acid Sequence, Bacterial Proteins genetics, Crystallography, X-Ray, Molecular Sequence Data, Repressor Proteins genetics, Sequence Analysis, DNA, Thermotoga maritima genetics, Bacterial Proteins chemistry, Models, Molecular, Repressor Proteins chemistry, Thermotoga maritima chemistry
Published
2007
Full Text
View/download PDF

12. Crystal structure of an ORFan protein (TM1622) from Thermotoga maritima at 1.75 A resolution reveals a fold similar to the Ran-binding protein Mog1p.

Author

Xu Q, Krishna SS, McMullan D, Schwarzenbacher R, Miller MD, Abdubek P, Agarwalla S, Ambing E, Astakhova T, Axelrod HL, Canaves JM, Carlton D, Chiu HJ, Clayton T, DiDonato M, Duan L, Elsliger MA, Feuerhelm J, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Koesema E, Kreusch A, Kuhn P, Morse AT, Nigoghossian E, Okach L, Oommachen S, Paulsen J, Quijano K, Reyes R, Rife CL, Spraggon G, Stevens RC, van den Bedem H, White A, Wolf G, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, and Wilson IA

Subjects
Amino Acid Sequence, Bacterial Proteins isolation & purification, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Protein Folding, Protein Structure, Secondary, Saccharomyces cerevisiae Proteins chemistry, Thermotoga maritima chemistry, ran GTP-Binding Protein chemistry, Bacterial Proteins chemistry, Thermotoga maritima enzymology
Published
2006
Full Text
View/download PDF

13. Comparative structural analysis of a novel glutathioneS-transferase (ATU5508) from Agrobacterium tumefaciens at 2.0 A resolution.

Author

Kosloff M, Han GW, Krishna SS, Schwarzenbacher R, Fasnacht M, Elsliger MA, Abdubek P, Agarwalla S, Ambing E, Astakhova T, Axelrod HL, Canaves JM, Carlton D, Chiu HJ, Clayton T, DiDonato M, Duan L, Feuerhelm J, Grittini C, Grzechnik SK, Hale J, Hampton E, Haugen J, Jaroszewski L, Jin KK, Johnson H, Klock HE, Knuth MW, Koesema E, Kreusch A, Kuhn P, Levin I, McMullan D, Miller MD, Morse AT, Moy K, Nigoghossian E, Okach L, Oommachen S, Page R, Paulsen J, Quijano K, Reyes R, Rife CL, Sims E, Spraggon G, Sridhar V, Stevens RC, van den Bedem H, Velasquez J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, and Wilson IA

Subjects
Agrobacterium tumefaciens chemistry, Agrobacterium tumefaciens cytology, Amino Acid Sequence, Bacterial Proteins classification, Crystallography, X-Ray, Dimerization, Glutathione Transferase classification, Models, Molecular, Molecular Sequence Data, Phylogeny, Protein Structure, Secondary, Agrobacterium tumefaciens enzymology, Bacterial Proteins chemistry, Glutathione Transferase chemistry
Abstract

Glutathione S-transferases (GSTs) comprise a diverse superfamily of enzymes found in organisms from all kingdoms of life. GSTs are involved in diverse processes, notably small-molecule biosynthesis or detoxification, and are frequently also used in protein engineering studies or as biotechnology tools. Here, we report the high-resolution X-ray structure of Atu5508 from the pathogenic soil bacterium Agrobacterium tumefaciens (atGST1). Through use of comparative sequence and structural analysis of the GST superfamily, we identified local sequence and structural signatures, which allowed us to distinguish between different GST classes. This approach enables GST classification based on structure, without requiring additional biochemical or immunological data. Consequently, analysis of the atGST1 crystal structure suggests a new GST class, distinct from previously characterized GSTs, which would make it an attractive target for further biochemical studies., ((c) 2006 Wiley-Liss, Inc.)

Published
2006
Full Text
View/download PDF

14. Crystal structure of 2-phosphosulfolactate phosphatase (ComB) from Clostridium acetobutylicum at 2.6 A resolution reveals a new fold with a novel active site.

Author

DiDonato M, Krishna SS, Schwarzenbacher R, McMullan D, Agarwalla S, Brittain SM, Miller MD, Abdubek P, Ambing E, Axelrod HL, Canaves JM, Chiu HJ, Deacon AM, Duan L, Elsliger MA, Godzik A, Grzechnik SK, Hale J, Hampton E, Haugen J, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Koesema E, Kreusch A, Kuhn P, Lesley SA, Levin I, Morse AT, Nigoghossian E, Okach L, Oommachen S, Paulsen J, Quijano K, Reyes R, Rife CL, Spraggon G, Stevens RC, van den Bedem H, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, and Wilson IA

Subjects
Acid Phosphatase isolation & purification, Amino Acid Sequence, Binding Sites, Clostridium acetobutylicum chemistry, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Folding, Acid Phosphatase chemistry, Clostridium acetobutylicum enzymology
Published
2006
Full Text
View/download PDF

15. Crystal structure of phosphoribosylformyl-glycinamidine synthase II, PurS subunit (TM1244) from Thermotoga maritima at 1.90 A resolution.

Author

Mathews II, Krishna SS, Schwarzenbacher R, McMullan D, Jaroszewski L, Miller MD, Abdubek P, Agarwalla S, Ambing E, Axelrod HL, Canaves JM, Carlton D, Chiu HJ, Clayton T, DiDonato M, Duan L, Elsliger MA, Grzechnik SK, Hale J, Hampton E, Haugen J, Jin KK, Klock HE, Koesema E, Kovarik JS, Kreusch A, Kuhn P, Levin I, Morse AT, Nigoghossian E, Okach L, Oommachen S, Paulsen J, Quijano K, Reyes R, Rife CL, Spraggon G, Stevens RC, van den Bedem H, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, and Wilson IA

Subjects
Amino Acid Sequence, Bacterial Proteins chemistry, Crystallization, Crystallography, X-Ray, Molecular Sequence Data, Protein Structure, Quaternary, Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor chemistry, Thermotoga maritima enzymology
Published
2006
Full Text
View/download PDF

16. Crystal structure of the ApbE protein (TM1553) from Thermotoga maritima at 1.58 A resolution.

Author

Han GW, Sri Krishna S, Schwarzenbacher R, McMullan D, Ginalski K, Elsliger MA, Brittain SM, Abdubek P, Agarwalla S, Ambing E, Astakhova T, Axelrod H, Canaves JM, Chiu HJ, DiDonato M, Grzechnik SK, Hale J, Hampton E, Haugen J, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Koesema E, Kreusch A, Kuhn P, Miller MD, Morse AT, Moy K, Nigoghossian E, Oommachen S, Ouyang J, Paulsen J, Quijano K, Reyes R, Rife C, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Wang X, West B, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, and Wilson IA

Subjects
Amino Acid Sequence, Crystallization, Crystallography, X-Ray, Molecular Sequence Data, Sequence Alignment, Bacterial Proteins chemistry, Lipoproteins chemistry, Thermotoga maritima chemistry
Published
2006
Full Text
View/download PDF

17. Crystal structure of acireductone dioxygenase (ARD) from Mus musculus at 2.06 angstrom resolution.

Author

Xu Q, Schwarzenbacher R, Krishna SS, McMullan D, Agarwalla S, Quijano K, Abdubek P, Ambing E, Axelrod H, Biorac T, Canaves JM, Chiu HJ, Elsliger MA, Grittini C, Grzechnik SK, DiDonato M, Hale J, Hampton E, Han GW, Haugen J, Hornsby M, Jaroszewski L, Klock HE, Knuth MW, Koesema E, Kreusch A, Kuhn P, Miller MD, Moy K, Nigoghossian E, Paulsen J, Reyes R, Rife C, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, White A, Wolf G, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, and Wilson IA

Subjects
Amino Acid Sequence, Animals, Binding Sites, Crystallization, Databases, Protein, Dioxygenases genetics, Dioxygenases metabolism, Metals chemistry, Mice, Models, Molecular, Molecular Sequence Data, Molecular Structure, Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary, Dioxygenases chemistry
Published
2006
Full Text
View/download PDF

18. Crystal structure of phosphoribosylformylglycinamidine synthase II (smPurL) from Thermotoga maritima at 2.15 A resolution.

Author

Mathews II, Krishna SS, Schwarzenbacher R, McMullan D, Abdubek P, Ambing E, Canaves JM, Chiu HJ, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Jaroszewski L, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, Levin I, Miller MD, Moy K, Nigoghossian E, Paulsen J, Quijano K, Reyes R, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, and Wilson IA

Subjects
Amino Acid Sequence, Binding Sites, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Protein Structure, Quaternary, Protein Structure, Tertiary, Structural Homology, Protein, Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor chemistry, Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor metabolism, Thermotoga maritima enzymology
Published
2006
Full Text
View/download PDF

19. Crystal structure of TM1367 from Thermotoga maritima at 1.90 A resolution reveals an atypical member of the cyclophilin (peptidylprolyl isomerase) fold.

Author

Jin KK, Krishna SS, Schwarzenbacher R, McMullan D, Abdubek P, Agarwalla S, Ambing E, Axelrod H, Canaves JM, Chiu HJ, Deacon AM, DiDonato M, Elsliger MA, Feuerhelm J, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Haugen J, Hornsby M, Jaroszewski L, Klock HE, Knuth MW, Koesema E, Kreusch A, Kuhn P, Lesley SA, Miller MD, Moy K, Nigoghossian E, Okach L, Oommachen S, Paulsen J, Quijano K, Reyes R, Rife C, Stevens RC, Spraggon G, van den Bedem H, Velasquez J, White A, Wolf G, Han GW, Xu Q, Hodgson KO, Wooley J, and Wilson IA

Subjects
Amino Acid Sequence, Bacterial Proteins genetics, Binding Sites, Crystallography, X-Ray, Humans, Models, Molecular, Molecular Sequence Data, Peptidylprolyl Isomerase classification, Polyethylene Glycols, Protein Folding, Protein Structure, Quaternary, Protein Structure, Tertiary, Bacterial Proteins chemistry, Bacterial Proteins metabolism, Cyclophilins chemistry, Cyclophilins metabolism, Peptidylprolyl Isomerase chemistry, Peptidylprolyl Isomerase metabolism, Thermotoga maritima enzymology
Published
2006
Full Text
View/download PDF

20. Crystal structure of a single-stranded DNA-binding protein (TM0604) from Thermotoga maritima at 2.60 A resolution.

Author

DiDonato M, Krishna SS, Schwarzenbacher R, McMullan D, Jaroszewski L, Miller MD, Abdubek P, Agarwalla S, Ambing E, Axelrod H, Biorac T, Chiu HJ, Deacon AM, Elsliger MA, Feuerhelm J, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Haugen J, Hornsby M, Klock HE, Knuth MW, Koesema E, Kreusch A, Kuhn P, Lesley SA, Moy K, Nigoghossian E, Okach L, Paulsen J, Quijano K, Reyes R, Rife C, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, and Wilson IA

Subjects
Amino Acid Sequence, Anisotropy, Crystallography, X-Ray, DNA, Single-Stranded, Escherichia coli metabolism, Mitochondria metabolism, Models, Molecular, Molecular Sequence Data, Plasmids metabolism, Protein Structure, Secondary, Transcription Factors chemistry, X-Ray Diffraction, DNA-Binding Proteins chemistry, Thermotoga maritima metabolism
Published
2006
Full Text
View/download PDF

21. Crystal structure of virulence factor CJ0248 from Campylobacter jejuni at 2.25 A resolution reveals a new fold.

Author

Xu Q, Schwarzenbacher R, McMullan D, Abdubek P, Agarwalla S, Ambing E, Axelrod H, Biorac T, Canaves JM, Chiu HJ, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Hornsby M, Jaroszewski L, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, Miller MD, Moy K, Nigoghossian E, Paulsen J, Quijano K, Reyes R, Rife C, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, White A, Wolf G, Hodgson KO, Wooley J, and Wilson IA

Subjects
Bacterial Proteins metabolism, Crystallography, X-Ray, Models, Molecular, Protein Folding, Protein Structure, Secondary, Virulence Factors metabolism, Bacterial Proteins chemistry, Campylobacter jejuni pathogenicity, Virulence Factors chemistry
Published
2006
Full Text
View/download PDF

22. Crystal structure of a conserved hypothetical protein (gi: 13879369) from Mouse at 1.90 A resolution reveals a new fold.

Author

Klock HE, Schwarzenbacher R, Xu Q, McMullan D, Abdubek P, Ambing E, Axelrod H, Biorac T, Canaves JM, Chiu HJ, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Hornsby M, Jaroszewski L, Koesema E, Kreusch A, Kuhn P, Miller MD, Moy K, Nigoghossian E, Paulsen J, Quijano K, Reyes R, Rife C, Sims E, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, White A, Wolf G, Hodgson KO, Wooley J, Lesley SA, and Wilson IA

Subjects
Animals, Conserved Sequence, Crystallography, X-Ray, Mice, Models, Molecular, Molecular Weight, Open Reading Frames, Protein Folding, Protein Structure, Secondary, Databases, Protein, Proteins chemistry
Published
2005
Full Text
View/download PDF

23. Crystal structure of Hsp33 chaperone (TM1394) from Thermotoga maritima at 2.20 A resolution.

Author

Jaroszewski L, Schwarzenbacher R, McMullan D, Abdubek P, Agarwalla S, Ambing E, Axelrod H, Biorac T, Canaves JM, Chiu HJ, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Hornsby M, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, Miller MD, Moy K, Nigoghossian E, Paulsen J, Quijano K, Reyes R, Rife C, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, and Wilson IA

Subjects
Amino Acid Sequence, Crystallization, Molecular Sequence Data, Zinc Fingers, Bacterial Proteins chemistry, Heat-Shock Proteins chemistry, Molecular Chaperones chemistry, Thermotoga maritima chemistry
Published
2005
Full Text
View/download PDF

24. Crystal structure of the global regulatory protein CsrA from Pseudomonas putida at 2.05 A resolution reveals a new fold.

Author

Rife C, Schwarzenbacher R, McMullan D, Abdubek P, Ambing E, Axelrod H, Biorac T, Canaves JM, Chiu HJ, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Hornsby M, Jaroszewski L, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, Miller MD, Moy K, Nigoghossian E, Paulsen J, Quijano K, Reyes R, Sims E, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, and Wilson IA

Subjects
Amino Acid Sequence, Crystallography, X-Ray, Dimerization, Molecular Sequence Data, Protein Folding, Bacterial Proteins chemistry, Models, Molecular, Pseudomonas putida, RNA-Binding Proteins chemistry
Published
2005
Full Text
View/download PDF

25. Crystal structure of a putative modulator of DNA gyrase (pmbA) from Thermotoga maritima at 1.95 A resolution reveals a new fold.

Author

Rife C, Schwarzenbacher R, McMullan D, Abdubek P, Ambing E, Axelrod H, Biorac T, Canaves JM, Chiu HJ, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Hornsby M, Jaroszewski L, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, Miller MD, Moy K, Nigoghossian E, Paulsen J, Quijano K, Reyes R, Sims E, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, and Wilson IA

Subjects
Amino Acid Sequence, Crystallography, X-Ray, DNA Gyrase metabolism, Dimerization, Molecular Sequence Data, Protein Folding, Bacterial Proteins chemistry, Models, Molecular, Thermotoga maritima enzymology
Published
2005
Full Text
View/download PDF

26. Crystal structure of an Apo mRNA decapping enzyme (DcpS) from Mouse at 1.83 A resolution.

Author

Han GW, Schwarzenbacher R, McMullan D, Abdubek P, Ambing E, Axelrod H, Biorac T, Canaves JM, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Haugen J, Hornsby M, Jaroszewski L, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, McPhillips TM, Miller MD, Moy K, Nigoghossian E, Paulsen J, Quijano K, Reyes R, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, and Wilson IA

Subjects
Amino Acid Sequence, Animals, Crystallography, X-Ray, Mice, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary, Sensitivity and Specificity, Apoenzymes chemistry, Endoribonucleases chemistry, RNA, Messenger metabolism
Published
2005
Full Text
View/download PDF

27. Crystal structure of S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA) from Thermotoga maritima at 2.0 A resolution reveals a new fold.

Author

Mathews I, Schwarzenbacher R, McMullan D, Abdubek P, Ambing E, Axelrod H, Biorac T, Canaves JM, Chiu HJ, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Hornsby M, Jaroszewski L, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, Levin I, Miller MD, Moy K, Nigoghossian E, Ouyang J, Paulsen J, Quijano K, Reyes R, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, and Wilson IA

Subjects
Crystallography, X-Ray methods, Isomerases metabolism, Ligands, Models, Molecular, Protein Conformation, Solvents, Isomerases chemistry, Protein Folding, Thermotoga maritima enzymology
Published
2005
Full Text
View/download PDF

28. Crystal structure of an indigoidine synthase A (IndA)-like protein (TM1464) from Thermotoga maritima at 1.90 A resolution reveals a new fold.

Author

Levin I, Miller MD, Schwarzenbacher R, McMullan D, Abdubek P, Ambing E, Biorac T, Cambell J, Canaves JM, Chiu HJ, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Hornsby M, Jaroszewski L, Karlak C, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, Morse A, Moy K, Nigoghossian E, Ouyang J, Page R, Quijano K, Reyes R, Robb A, Sims E, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, Wang X, West B, Wolf G, Xu Q, Zagnitko O, Hodgson KO, Wooley J, and Wilson IA

Subjects
Bacterial Proteins metabolism, Crystallography, X-Ray, Models, Molecular, Piperidones metabolism, Protein Conformation, Protein Folding, Bacterial Proteins chemistry, Thermotoga maritima enzymology
Published
2005
Full Text
View/download PDF

29. Crystal structure of a formiminotetrahydrofolate cyclodeaminase (TM1560) from Thermotoga maritima at 2.80 A resolution reveals a new fold.

Author

Xu Q, Schwarzenbacher R, McMullan D, Abdubek P, Ambing E, Biorac T, Canaves JM, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hampton E, Hornsby M, Jaroszewski L, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, Levin I, Miller MD, Morse A, Moy K, Ouyang J, Page R, Quijano K, Reyes R, Robb A, Sims E, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, von Delft F, Wang X, West B, White A, Wolf G, Zagnitko O, Hodgson KO, Wooley J, and Wilson IA

Subjects
Amino Acid Sequence, Binding Sites, Crystallization, Crystallography, X-Ray, Enzyme Stability, Models, Chemical, Models, Molecular, Molecular Conformation, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Ammonia-Lyases chemistry, Thermotoga maritima enzymology
Published
2005
Full Text
View/download PDF

30. Crystal structure of an alanine-glyoxylate aminotransferase from Anabaena sp. at 1.70 A resolution reveals a noncovalently linked PLP cofactor.

Author

Han GW, Schwarzenbacher R, Page R, Jaroszewski L, Abdubek P, Ambing E, Biorac T, Canaves JM, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Haugen J, Hornsby M, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, Levin I, McMullan D, McPhillips TM, Miller MD, Morse A, Moy K, Nigoghossian E, Ouyang J, Paulsen J, Quijano K, Reyes R, Sims E, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, von Delft F, Wang X, West B, White A, Wolf G, Xu Q, Zagnitko O, Hodgson KO, Wooley J, and Wilson IA

Subjects
Amino Acid Sequence, Crystallography, X-Ray, Electrons, Humans, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Stereoisomerism, Anabaena enzymology, Proteins chemistry, Transaminases chemistry
Published
2005
Full Text
View/download PDF

31. Crystal structure of an alpha/beta serine hydrolase (YDR428C) from Saccharomyces cerevisiae at 1.85 A resolution.

Author

Arndt JW, Schwarzenbacher R, Page R, Abdubek P, Ambing E, Biorac T, Canaves JM, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Hornsby M, Klock HE, Koesema E, Kreusch A, Kuhn P, Jaroszewski L, Lesley SA, Levin I, McMullan D, McPhillips TM, Miller MD, Morse A, Moy K, Nigoghossian E, Ouyang J, Peti WS, Quijano K, Reyes R, Sims E, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, von Delft F, Wang X, West B, White A, Wolf G, Xu Q, Zagnitko O, Hodgson KO, Wooley J, and Wilson IA

Subjects
Amino Acid Sequence, Binding Sites, Computational Biology, Models, Molecular, Molecular Conformation, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Software, Crystallography, X-Ray methods, Hydrolases chemistry, Saccharomyces cerevisiae metabolism, Saccharomyces cerevisiae Proteins chemistry, Serine chemistry
Published
2005
Full Text
View/download PDF

32. Crystal structure of a tandem cystathionine-beta-synthase (CBS) domain protein (TM0935) from Thermotoga maritima at 1.87 A resolution.

Author

Miller MD, Schwarzenbacher R, von Delft F, Abdubek P, Ambing E, Biorac T, Brinen LS, Canaves JM, Cambell J, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Eshagi S, Floyd R, Godzik A, Grittini C, Grzechnik SK, Hampton E, Jaroszewski L, Karlak C, Klock HE, Koesema E, Kovarik JS, Kreusch A, Kuhn P, Lesley SA, Levin I, McMullan D, McPhillips TM, Morse A, Moy K, Ouyang J, Page R, Quijano K, Robb A, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, Wang X, West B, Wolf G, Xu Q, Hodgson KO, Wooley J, and Wilson IA

Subjects
Amino Acid Sequence, Crystallography, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary, Protein Structure, Tertiary, Bacterial Proteins chemistry, Cystathionine beta-Synthase chemistry, Thermotoga maritima enzymology
Published
2004
Full Text
View/download PDF

33. Crystal structure of a putative NADPH-dependent oxidoreductase (GI: 18204011) from mouse at 2.10 A resolution.

Author

Levin I, Schwarzenbacher R, McMullan D, Abdubek P, Ambing E, Biorac T, Cambell J, Canaves JM, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hampton E, Jaroszewski L, Karlak C, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, McPhillips TM, Miller MD, Morse A, Moy K, Ouyang J, Page R, Quijano K, Reyes R, Robb A, Sims E, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, von Delft F, Wang X, West B, Wolf G, Xu Q, Hodgson KO, Wooley J, and Wilson IA

Subjects
Amino Acid Sequence, Animals, Binding Sites, Crystallography, X-Ray, Mice, Models, Molecular, Molecular Sequence Data, NADP metabolism, Oxidoreductases metabolism, Protein Structure, Secondary, Protein Structure, Tertiary, Quinone Reductases chemistry, Structural Homology, Protein, Oxidoreductases chemistry
Published
2004
Full Text
View/download PDF

34. Crystal structure of an allantoicase (YIR029W) from Saccharomyces cerevisiae at 2.4 A resolution.

Author

Xu Q, Schwarzenbacher R, Page R, Sims E, Abdubek P, Ambing E, Biorac T, Brinen LS, Cambell J, Canaves JM, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Floyd R, Godzik A, Grittini C, Grzechnik SK, Hampton E, Jaroszewski L, Karlak C, Klock HE, Koesema E, Kovarik JS, Kreusch A, Kuhn P, Lesley SA, Levin I, McMullan D, McPhillips TM, Miller MD, Morse A, Moy K, Ouyang J, Quijano K, Reyes R, Rezezadeh F, Robb A, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, von Delft F, Wang X, West B, Wolf G, Hodgson KO, Wooley J, and Wilson IA

Subjects
Amino Acid Sequence, Conserved Sequence, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Multienzyme Complexes, Protein Structure, Secondary, Protein Structure, Tertiary, Structural Homology, Protein, Saccharomyces cerevisiae enzymology, Ureohydrolases chemistry
Published
2004
Full Text
View/download PDF

35. Crystal structure of a novel Thermotoga maritima enzyme (TM1112) from the cupin family at 1.83 A resolution.

Author

McMullan D, Schwarzenbacher R, Jaroszewski L, von Delft F, Klock HE, Vincent J, Quijano K, Abdubek P, Ambing E, Biorac T, Brinen LS, Canaves JM, Dai X, Deacon AM, DiDonato M, Elsliger MA, Eshaghi S, Floyd R, Godzik A, Grittini C, Grzechnik SK, Hampton E, Karlak C, Koesema E, Kreusch A, Kuhn P, Levin I, McPhillips TM, Miller MD, Morse A, Moy K, Ouyang J, Page R, Reyes R, Rezezadeh F, Robb A, Sims E, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Wang X, West B, Wolf G, Xu Q, Hodgson KO, Wooley J, Lesley SA, and Wilson IA

Subjects
Amino Acid Sequence, Binding Sites, Conserved Sequence, Crystallization, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary, Structural Homology, Protein, Bacterial Proteins chemistry, Thermotoga maritima enzymology
Published
2004
Full Text
View/download PDF

36. Crystal structure of a PIN (PilT N-terminus) domain (AF0591) from Archaeoglobus fulgidus at 1.90 A resolution.

Author

Levin I, Schwarzenbacher R, Page R, Abdubek P, Ambing E, Biorac T, Brinen LS, Campbell J, Canaves JM, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Floyd R, Godzik A, Grittini C, Grzechnik SK, Hampton E, Jaroszewski L, Karlak C, Klock HE, Koesema E, Kovarik JS, Kreusch A, Kuhn P, Lesley SA, McMullan D, McPhillips TM, Miller MD, Morse A, Moy K, Ouyang J, Quijano K, Reyes R, Rezezadeh F, Robb A, Sims E, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, von Delft F, Wang X, West B, Wolf G, Xu Q, Hodgson KO, Wooley J, and Wilson IA

Subjects
Amino Acid Sequence, Binding Sites, Crystallography, X-Ray, Exonucleases chemistry, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Siphoviridae enzymology, Viral Proteins chemistry, Archaeal Proteins chemistry, Archaeoglobus fulgidus chemistry
Published
2004
Full Text
View/download PDF

37. Crystal structure of a putative oxalate decarboxylase (TM1287) from Thermotoga maritima at 1.95 A resolution.

Author

Schwarzenbacher R, von Delft F, Jaroszewski L, Abdubek P, Ambing E, Biorac T, Brinen LS, Canaves JM, Cambell J, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Eshagi S, Floyd R, Godzik A, Grittini C, Grzechnik SK, Hampton E, Karlak C, Klock HE, Koesema E, Kovarik JS, Kreusch A, Kuhn P, Lesley SA, Levin I, McMullan D, McPhillips TM, Miller MD, Morse A, Moy K, Ouyang J, Page R, Quijano K, Robb A, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, Wang X, West B, Wolf G, Xu Q, Hodgson KO, Wooley J, and Wilson IA

Subjects
Amino Acid Sequence, Bacterial Proteins genetics, Bacterial Proteins metabolism, Carboxy-Lyases genetics, Carboxy-Lyases metabolism, Crystallography, X-Ray, Ligands, Models, Molecular, Molecular Sequence Data, Multigene Family, Oxalates metabolism, Protein Conformation, Protein Structure, Secondary, Proteome, Recombinant Fusion Proteins chemistry, Thermotoga maritima genetics, Bacterial Proteins chemistry, Carboxy-Lyases chemistry, Thermotoga maritima enzymology
Published
2004
Full Text
View/download PDF

38. Crystal structure of an Udp-n-acetylmuramate-alanine ligase MurC (TM0231) from Thermotoga maritima at 2.3 A resolution.

Author

Spraggon G, Schwarzenbacher R, Kreusch A, Lee CC, Abdubek P, Ambing E, Biorac T, Brinen LS, Canaves JM, Cambell J, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Eshagi S, Floyd R, Godzik A, Grittini C, Grzechnik SK, Hampton E, Jaroszewski L, Karlak C, Klock HE, Koesema E, Kovarik JS, Kuhn P, Levin I, McMullan D, McPhillips TM, Miller MD, Morse A, Moy K, Ouyang J, Page R, Quijano K, Robb A, Stevens RC, van den Bedem H, Velasquez J, Vincent J, von Delft F, Wang X, West B, Wolf G, Xu Q, Hodgson KO, Wooley J, Lesley SA, and Wilson IA

Subjects
Amino Acid Sequence, Crystallography, X-Ray, Molecular Sequence Data, Bacterial Proteins chemistry, Models, Molecular, Peptide Synthases chemistry, Thermotoga maritima enzymology
Published
2004
Full Text
View/download PDF

39. Crystal structure of an aspartate aminotransferase (TM1255) from Thermotoga maritima at 1.90 A resolution.

Author

Schwarzenbacher R, Jaroszewski L, von Delft F, Abdubek P, Ambing E, Biorac T, Brinen LS, Canaves JM, Cambell J, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Eshagi S, Floyd R, Godzik A, Grittini C, Grzechnik SK, Hampton E, Karlak C, Klock HE, Koesema E, Kovarik JS, Kreusch A, Kuhn P, Lesley SA, Levin I, McMullan D, McPhillips TM, Miller MD, Morse A, Moy K, Ouyang J, Page R, Quijano K, Robb A, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, Wang X, West B, Wolf G, Xu Q, Hodgson KO, Wooley J, and Wilson IA

Subjects
Amino Acid Sequence, Crystallography, X-Ray, Molecular Sequence Data, Aspartate Aminotransferases chemistry, Bacterial Proteins chemistry, Models, Molecular, Thermotoga maritima enzymology
Published
2004
Full Text
View/download PDF

40. Crystal structure of a type II quinolic acid phosphoribosyltransferase (TM1645) from Thermotoga maritima at 2.50 A resolution.

Author

Schwarzenbacher R, Jaroszewski L, von Delft F, Abdubek P, Ambing E, Biorac T, Brinen LS, Canaves JM, Cambell J, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Eshagi S, Floyd R, Godzik A, Grittini C, Grzechnik SK, Hampton E, Karlak C, Klock HE, Koesema E, Kovarik JS, Kreusch A, Kuhn P, Lesley SA, Levin I, McMullan D, McPhillips TM, Miller MD, Morse A, Moy K, Ouyang J, Page R, Quijano K, Robb A, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, Wang X, West B, Wolf G, Xu Q, Hodgson KO, Wooley J, and Wilson IA

Subjects
Amino Acid Sequence, Crystallography, X-Ray, Dimerization, Molecular Sequence Data, Bacterial Proteins chemistry, Models, Molecular, Pentosyltransferases chemistry, Thermotoga maritima enzymology
Published
2004
Full Text
View/download PDF

41. Crystal structure of a phosphoribosylaminoimidazole mutase PurE (TM0446) from Thermotoga maritima at 1.77-A resolution.

Author

Schwarzenbacher R, Jaroszewski L, von Delft F, Abdubek P, Ambing E, Biorac T, Brinen LS, Canaves JM, Cambell J, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Eshagi S, Floyd R, Godzik A, Grittini C, Grzechnik SK, Hampton E, Karlak C, Klock HE, Koesema E, Kovarik JS, Kreusch A, Kuhn P, Lesley SA, Levin I, McMullan D, McPhillips TM, Miller MD, Morse A, Moy K, Ouyang J, Page R, Quijano K, Robb A, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, Wang X, West B, Wolf G, Xu Q, Hodgson KO, Wooley J, and Wilson IA

Subjects
Amino Acid Sequence, Crystallization, Crystallography, X-Ray, Intramolecular Transferases metabolism, Models, Molecular, Molecular Sequence Data, Protein Conformation, Reproducibility of Results, Imidazoles metabolism, Intramolecular Transferases chemistry, Thermotoga maritima enzymology
Published
2004
Full Text
View/download PDF

42. Crystal structure of a putative PII-like signaling protein (TM0021) from Thermotoga maritima at 2.5 A resolution.

Author

Schwarzenbacher R, von Delft F, Abdubek P, Ambing E, Biorac T, Brinen LS, Canaves JM, Cambell J, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Eshagi S, Floyd R, Godzik A, Grittini C, Grzechnik SK, Hampton E, Jaroszewski L, Karlak C, Klock HE, Koesema E, Kovarik JS, Kreusch A, Kuhn P, Lesley SA, Levin I, McMullan D, McPhillips TM, Miller MD, Morse A, Moy K, Ouyang J, Page R, Quijano K, Robb A, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, Wang X, West B, Wolf G, Xu Q, Hodgson KO, Wooley J, and Wilson IA

Subjects
Amino Acid Sequence, Bacterial Proteins genetics, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, PII Nitrogen Regulatory Proteins, Protein Structure, Secondary, Reproducibility of Results, Thermotoga maritima genetics, Bacterial Proteins chemistry, Signal Transduction, Thermotoga maritima chemistry
Published
2004
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results