Author:
McHugh Colin S.,Cook Paul D.
Abstract
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 Å 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.
Funder
National Institute of General Medical Sciences
Publisher
International Union of Crystallography (IUCr)
Subject
Condensed Matter Physics,Genetics,Biochemistry,Structural Biology,Biophysics
Cited by
1 articles.
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