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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.

Authors :
Myung Choi J
Cao TP
Wouk Kim S
Ho Lee K
Haeng Lee S
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.)

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