title: MxaJ structure reveals a periplasmic binding protein-like architecture with unique secondary structural elements.
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 cL. 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.
authors.affiliation: Department of Cellular and Molecular Medicine, Chosun University School of Medicine, Gwangju, 61452, Korea.
authors.forename: Jin
authors.initials: J
authors.lastname: Myung Choi
authors.affiliation: Department of Cellular and Molecular Medicine, Chosun University School of Medicine, Gwangju, 61452, Korea.|National Research Center for Dementia, Chosun University, Gwangju, 61452, Korea.
authors.forename: Thinh-Phat
authors.initials: TP
authors.lastname: Cao
authors.affiliation: Department of Environmental Engineering, Chosun University, Gwangju, 61452, Korea.
authors.forename: Si
authors.initials: S
authors.lastname: Wouk Kim
authors.affiliation: National Research Center for Dementia, Chosun University, Gwangju, 61452, Korea.
authors.forename: Kun
authors.initials: K
authors.lastname: Ho Lee
authors.affiliation: Department of Cellular and Molecular Medicine, Chosun University School of Medicine, Gwangju, 61452, Korea.
authors.forename: Sung
authors.identifier: 0000-0002-6658-9714
authors.initials: S
authors.lastname: Haeng Lee
mesh_terms: D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D003574:Cytochrome c Group / Q000737:chemistry* / Q000378:metabolism; D004579:Electron Transport; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D008024:Ligands; D000432:Methanol / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D010084:Oxidation-Reduction; D044147:Piscirickettsiaceae / Q000737:chemistry* / Q000201:enzymology; D011485:Protein Binding; D000072756:Protein Conformation, alpha-Helical; D000072757:Protein Conformation, beta-Strand; D017510:Protein Folding; D054730:Protein Interaction Domains and Motifs; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D001426:Bacterial Proteins; D003574:Cytochrome c Group; D008024:Ligands; D011994:Recombinant Proteins; C058498:cytochrome C(L); D000429:Alcohol Oxidoreductases; C019641:alcohol dehydrogenase (acceptor); D000432:Methanol
keywords: Methylophaga aminisulfidivorans MPT; X-ray crystallography; methanol dehydrogenase; methanol oxidizing (mox) system; methanotrophs