5SV6

Crystal structure of MxaJ from Methlophaga aminisulfidivorans MPT

Summary for 5SV6

• Entry DOI: 10.2210/pdb5sv6/pdb
• Descriptor: Extracellular solute-binding protein, family 3, BROMIDE ION (3 entities in total)
• Functional Keywords: mxaj, methlophaga aminisulfidivorans, mdh, pbp, unknown function
• Biological source: Methylophaga aminisulfidivorans MP
• Total number of polymer chains: 1
• Total formula weight: 32919.78

Authors

Choi, J.M.,Lee, S.H. (deposition date: 2016-08-04, release date: 2017-07-12, Last modification date: 2024-11-20)

Primary citation

Choi, J.M.,Cao, T.P.,Kim, S.W.,Lee, K.H.,Lee, S.H.
MxaJ structure reveals a periplasmic binding protein-like architecture with unique secondary structural elements
Proteins, 85:1379-1386, 2017

PubMed 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 c . 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.

PubMed: 28295618
DOI: 10.1002/prot.25283

Experimental method

X-RAY DIFFRACTION (1.92 Å)