Structure of BrxA from Staphylococcus aureus, a bacilliredoxin involved in redox homeostasis in Firmicutes

被引：1

作者：

McHugh, Colin S. ^{[1
]}

Cook, Paul D. ^{[1
]}

机构：

[1] Grand Valley State Univ, Dept Chem, 1 Campus Dr, Allendale, MI 49401 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2022年 / 78卷

关键词：

BrxA; Staphylococcus aureus; bacillithiol; thioredoxins; Gram-positive bacteria; oxidative stress; redox homeostasis; BACILLITHIOL; THIOREDOXINS;

D O I：

10.1107/S2053230X22002400

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Bacilliredoxins are small proteins that are involved in redox homeostasis in bacillithiol-producing bacteria. They reduce mixed bacillithiol disulfides on protected proteins through a disulfide-exchange reaction, restoring the thiol group on the target protein. Bacilliredoxins contain an unusual conserved CGC motif, and their exact catalytic mechanism remains unclear. Here, a 1.6 angstrom resolution X-ray crystallographic structure of the bacilliredoxin BrxA (YphP) from Staphylococcus aureus is presented. The structure contains bacillithiol in a mixed disulfide with Cys54, as well as a disulfide linkage at Cys56, which may play a role in dimer stabilization. The structure presented here will provide insight into the function of BrxA and other bacilliredoxins.

引用

页码：144 / 149

页数：6

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