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MxaJ structure reveals a periplasmic binding protein-like architecture with unique secondary structural elements.
MxaJ structure reveals a periplasmic binding protein-like architecture with unique secondary structural elements.
- Source :
-
Proteins [Proteins] 2017 Jul; Vol. 85 (7), pp. 1379-1386. Date of Electronic Publication: 2017 Apr 07. - Publication Year :
- 2017
-
Abstract
- MxaJ is a component of type II methanol dehydrogenase (MDH) that mediates electron transfer during methanol oxidation in methanotrophic bacteria. However, little is known about how MxaJ structurally cooperates with MDH and Cytochrome c <subscript>L</subscript> . Here, we report for the first time the crystal structure of MxaJ. MxaJ consists of eight α-helices and six β-strands, and resembles the "bi-lobate" folding architecture found in periplasmic binding proteins. Distinctive features of MxaJ include prominent loops and a β-strand around the hinge region supporting the ligand-binding cavity, which might provide a more favorable framework for interacting with proteins rather than small molecules. Proteins 2017; 85:1379-1386. © 2017 Wiley Periodicals, Inc.<br /> (© 2017 Wiley Periodicals, Inc.)
- Subjects :
- Alcohol Oxidoreductases genetics
Alcohol Oxidoreductases metabolism
Amino Acid Sequence
Bacterial Proteins genetics
Bacterial Proteins metabolism
Binding Sites
Cloning, Molecular
Crystallography, X-Ray
Cytochrome c Group metabolism
Electron Transport
Escherichia coli genetics
Escherichia coli metabolism
Gene Expression
Ligands
Methanol metabolism
Models, Molecular
Oxidation-Reduction
Piscirickettsiaceae enzymology
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Folding
Protein Interaction Domains and Motifs
Protein Structure, Tertiary
Recombinant Proteins chemistry
Recombinant Proteins genetics
Recombinant Proteins metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Alcohol Oxidoreductases chemistry
Bacterial Proteins chemistry
Cytochrome c Group chemistry
Methanol chemistry
Piscirickettsiaceae chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1097-0134
- Volume :
- 85
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- Proteins
- Publication Type :
- Academic Journal
- Accession number :
- 28295618
- Full Text :
- https://doi.org/10.1002/prot.25283