MxaJ structure reveals a periplasmic binding protein-like architecture with unique secondary structural elements

Jin Myung Choi, Thinh Phat Cao, Si Wouk Kim, Kun Ho Lee, Sung Haeng Lee

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9 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)1379-1386
Number of pages8
JournalProteins: Structure, Function and Bioinformatics
Issue number7
Publication statusPublished - 1 Jul 2017
Externally publishedYes


  • methanol dehydrogenase
  • methanol oxidizing (mox) system
  • methanotrophs
  • Methylophaga aminisulfidivorans MP
  • X-ray crystallography

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