Structure and function of the bacillithiol‐ S ‐transferase BstA from Staphylococcus aureus
Abstract
Abstract 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.
- Authors:
-
- Department of Chemistry Grand Valley State University Allendale Michigan 49401
- Publication Date:
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1422461
- Grant/Contract Number:
- DE‐AC02‐06CH11357
- Resource Type:
- Publisher's Accepted Manuscript
- Journal Name:
- Protein Science
- Additional Journal Information:
- Journal Name: Protein Science Journal Volume: 27 Journal Issue: 4; Journal ID: ISSN 0961-8368
- Publisher:
- Wiley Blackwell (John Wiley & Sons)
- Country of Publication:
- United Kingdom
- Language:
- English
Citation Formats
Francis, Joel W., Royer, Christopher J., and Cook, Paul D. Structure and function of the bacillithiol‐ S ‐transferase BstA from Staphylococcus aureus. United Kingdom: N. p., 2018.
Web. doi:10.1002/pro.3384.
Francis, Joel W., Royer, Christopher J., & Cook, Paul D. Structure and function of the bacillithiol‐ S ‐transferase BstA from Staphylococcus aureus. United Kingdom. https://doi.org/10.1002/pro.3384
Francis, Joel W., Royer, Christopher J., and Cook, Paul D. Fri .
"Structure and function of the bacillithiol‐ S ‐transferase BstA from Staphylococcus aureus". United Kingdom. https://doi.org/10.1002/pro.3384.
@article{osti_1422461,
title = {Structure and function of the bacillithiol‐ S ‐transferase BstA from Staphylococcus aureus},
author = {Francis, Joel W. and Royer, Christopher J. and Cook, Paul D.},
abstractNote = {Abstract 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.},
doi = {10.1002/pro.3384},
journal = {Protein Science},
number = 4,
volume = 27,
place = {United Kingdom},
year = {Fri Feb 23 00:00:00 EST 2018},
month = {Fri Feb 23 00:00:00 EST 2018}
}
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