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MxaJ structure reveals a periplasmic binding protein‐like architecture with unique secondary structural elements
Author(s) -
Myung Choi Jin,
Cao ThinhPhat,
Wouk Kim Si,
Ho Lee Kun,
Haeng Lee Sung
Publication year - 2017
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25283
Subject(s) - periplasmic space , folding (dsp implementation) , chemistry , transmembrane protein , electron transfer , cytochrome , cytochrome c , crystallography , protein folding , biophysics , biochemistry , stereochemistry , biology , enzyme , photochemistry , receptor , escherichia coli , electrical engineering , mitochondrion , gene , engineering
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 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.