5sv6

Publication Abstract from PubMed

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 cL . Here, we report for the first time the crystal structure of MxaJ. MxaJ consists of eight alpha-helices and six beta-strands, and resembles the "bi-lobate" folding architecture found in periplasmic binding proteins. Distinctive features of MxaJ include prominent loops and a beta-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. (c) 2017 Wiley Periodicals, Inc.

MxaJ structure reveals a periplasmic binding protein-like architecture with unique secondary structural elements.,Myung Choi J, Cao TP, Wouk Kim S, Ho Lee K, Haeng Lee S Proteins. 2017 Jul;85(7):1379-1386. doi: 10.1002/prot.25283. Epub 2017 Apr 7. PMID:28295618^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.