Structure of YffB Protein from Brucella melitensis
Author Information
Author(s): Garry W. Buchko, Stephen N. Hewitt, Alberto J. Napuli, Wesley C. Van Voorhis, Peter J. Myler
Primary Institution: Seattle Structural Genomics Center for Infectious Disease
Hypothesis
The ArsC-YffB family of proteins may function as glutathione-dependent thiol reductases.
Conclusion
The structure of Bm-YffB is similar to that of other arsenate reductases, suggesting it may have a role in arsenate reduction.
Supporting Evidence
- B. melitensis is a potential agent for biological warfare.
- The protein Bm-YffB is a potential drug target.
- Chemical shift perturbation studies indicate that Bm-YffB binds reduced glutathione.
- The structure of Bm-YffB is similar to that of Pseudomonas aeruginosa YffB.
Takeaway
Scientists studied a protein from a bacteria that can help it survive arsenic, which is toxic. They found out how this protein is built and how it might work.
Methodology
The structure was determined using size-exclusion chromatography and NMR spectroscopy.
Limitations
The study does not explore the biochemical functions of Bm-YffB in detail.
Digital Object Identifier (DOI)
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