7CTO

Staphylococcus aureus MsrB

7CTO の概要

• エントリーDOI: 10.2210/pdb7cto/pdb
• 分子名称: Peptide methionine sulfoxide reductase MsrB (1 entity in total)
• 機能のキーワード: oxidoreductase, methionine sulfoxide reductase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 109946.05

構造登録者

Kim, H.J. (登録日: 2020-08-19, 公開日: 2020-10-07, 最終更新日: 2023-11-29)

主引用文献

Kim, H.J.
Implication of Staphylococcus aureus MsrB dimerization upon oxidation.
Biochem.Biophys.Res.Commun., 533:118-124, 2020

PubMed Abstract: Oxidative modification of protein structure has been shown to play a significant role in bacterial virulence and metabolism. The sulfur-containing residues are susceptible to oxidation and the enzymatic reversal of oxidized cysteine or methionine is detected in many organisms. Methionine sulfoxide reductases (Msr) are responsible for reducing oxidized methionine. The two different Msrs, MsrA and MsrB, reduce methionine R-sulfoxide and methionine S-sulfoxide, respectively through self-oxidation. This study elucidated the structure of MsrB from Staphylococcus aureus Mu50 and its changes upon oxidation. The active site shows two reduced cysteines in a close contact, implying disulfide bond would form without major structural rearrangement. When the protein is exposed to an oxidative condition, a dimeric state is observed. The dimerization of MsrB creates a valley structure for accepting peptidyl substrates. To the best of our knowledge, oxidation induced dimerization of MsrB would help to understand mechanism behind redox control that has not been well characterized.

PubMed: 32943184
DOI: 10.1016/j.bbrc.2020.08.070

実験手法

X-RAY DIFFRACTION (3.47 Å)