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Structure and function of the bacillithiol‐ S ‐transferase BstA from Staphylococcus aureus
Author(s) -
Francis Joel W.,
Royer Christopher J.,
Cook Paul D.
Publication year - 2018
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3384
Subject(s) - staphylococcus aureus , transferase , microbiology and biotechnology , chemistry , physics , computational biology , biology , biochemistry , bacteria , genetics , enzyme
Bacillithiol is a low‐molecular weight thiol produced by many gram‐positive organisms, including Staphylococcus aureus and Bacillus anthracis . It is the major thiol responsible for maintaining redox homeostasis and cellular detoxification, including inactivation of the antibiotic fosfomycin. The metal‐dependent bacillithiol transferase BstA is likely involved in these sorts of detoxification processes, but the exact substrates and enzyme mechanism have not been identified. Here we report the 1.34 Å resolution X‐ray crystallographic structure of BstA from S. aureus . Our structure confirms that BstA belongs to the YfiT‐like metal‐dependent hydrolase superfamily. Like YfiT, our structure contains nickel within its active site, but our functional data suggest that BstA utilizes zinc for activity. Although BstA and YfiT both contain a core four helix bundle and coordinate their metal ions in the same fashion, significant differences between the protein structures are described here.