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Structure and function of the bacillithiol-S-transferase BstA from Staphylococcus aureus
Joel W Francis1, Christopher J Royer1, Paul D Cook1
1Department of Chemistry, Grand Valley State University, Allendale, Michigan, 49401.
Protein Science : a Publication of the Protein Society
|February 9, 2018
Summary
Bacillithiol, crucial for bacterial detoxification and antibiotic resistance in organisms like Staphylococcus aureus, has its key enzyme BstA structurally characterized. Functional studies reveal BstA uses zinc, despite structural nickel presence, offering insights into bacterial defense mechanisms.
Area of Science:
- Biochemistry
- Structural Biology
- Microbiology
Background:
- Bacillithiol is a vital low-molecular weight thiol in Gram-positive bacteria, essential for redox homeostasis and cellular detoxification.
- It plays a role in inactivating antibiotics like fosfomycin.
- The bacillithiol transferase BstA is implicated in these detoxification processes, but its substrates and mechanism remain unclear.
Purpose of the Study:
- To determine the high-resolution X-ray crystallographic structure of BstA from Staphylococcus aureus.
- To investigate the metal ion utilized by BstA for its enzymatic activity.
- To elucidate the structural basis of BstA function within the YfiT-like hydrolase superfamily.
Main Methods:
- X-ray crystallography at 1.34 Å resolution.
- Biochemical assays to determine metal ion dependency.
- Comparative structural analysis with related enzymes.
Main Results:
- The crystal structure of S. aureus BstA was determined.
- BstA belongs to the YfiT-like metal-dependent hydrolase superfamily.
- While the structure contains nickel, functional data indicate BstA activity is dependent on zinc.
- Structural similarities and key differences between BstA and YfiT were identified.
Conclusions:
- The high-resolution structure of BstA provides a molecular basis for understanding its role in bacillithiol metabolism.
- BstA's differential metal ion utilization (structural nickel vs. functional zinc) highlights unique enzymatic properties.
- This work advances knowledge of bacterial detoxification pathways and potential antibiotic resistance mechanisms.
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