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From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
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MxaJ structure reveals a periplasmic binding protein-like architecture with unique secondary structural elements.

Jin Myung Choi1, Thinh-Phat Cao1,2, Si Wouk Kim3

  • 1Department of Cellular and Molecular Medicine, Chosun University School of Medicine, Gwangju, 61452, Korea.

Proteins
|March 16, 2017
PubMed
Summary

The crystal structure of MxaJ, a key protein in methanol oxidation, reveals a unique architecture. This structure suggests MxaJ may interact with other proteins, like MDH, rather than small molecules.

Keywords:
Methylophaga aminisulfidivorans MPTX-ray crystallographymethanol dehydrogenasemethanol oxidizing (mox) systemmethanotrophs

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • MxaJ is essential for electron transfer in type II methanol dehydrogenase (MDH).
  • The structural cooperation of MxaJ with MDH and Cytochrome cL is not well understood.

Purpose of the Study:

  • To determine the crystal structure of MxaJ.
  • To elucidate the structural basis for MxaJ's interactions within the MDH complex.

Main Methods:

  • X-ray crystallography was used to determine the MxaJ structure.

Main Results:

  • The crystal structure of MxaJ was determined for the first time.
  • MxaJ exhibits a bi-lobate folding architecture, similar to periplasmic binding proteins.
  • Prominent loops and a β-strand at the hinge region suggest protein-protein interaction capabilities.

Conclusions:

  • The MxaJ structure provides insights into its role in methanol oxidation.
  • MxaJ's structural features indicate a potential role in protein-protein interactions within the MDH complex.