期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 85, 期 7, 页码 1379-1386出版社
WILEY
DOI: 10.1002/prot.25283
关键词
methanol oxidizing (mox) system; methanol dehydrogenase; X-ray crystallography; methanotrophs; Methylophaga aminisulfidivorans MPT
资金
- Chosun University
- Brain Research Program through the National Research Foundation of Korea - Ministry of Science, ICT AMP
- Future Planning [NRF-2014M3C7A1046041]
- National Research Foundation of Korea [2014M3C7A1046041, 22A20130012098] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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(L). Here, we report for the first time the crystal structure of MxaJ. MxaJ consists of eight -helices and six -strands, and resembles the bi-lobate folding architecture found in periplasmic binding proteins. Distinctive features of MxaJ include prominent loops and a -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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据