Structures of a putative ζ-class glutathione S-transferase from the pathogenic fungus Coccidioides immitis
Author Information
Author(s): Edwards Thomas E., Bryan Cassie M., Leibly David J., Dieterich Shellie H., Abendroth Jan, Sankaran Banumathi, Sivam Dhileep, Staker Bart L., Van Voorhis Wesley C., Myler Peter J., Stewart Lance J.
Primary Institution: Seattle Structural Genomics Center for Infectious Disease
Hypothesis
The protein investigated is likely to be a ζ-class glutathione S-transferase based on its sequence homology and structural characteristics.
Conclusion
The study presents two crystal structures of a putative uncharacterized protein from C. immitis, suggesting it is a ζ-class GST/MAAI.
Supporting Evidence
- The protein shares sequence similarity with known ζ-class glutathione S-transferases.
- Two crystal structures were determined: one apo and one glutathione-bound.
- The apo structure reveals a nonsymmetric homodimer.
- Half-site binding of glutathione was observed in the glutathione-bound form.
- Significant movement of active site components was noted upon glutathione binding.
Takeaway
Scientists studied a protein from a fungus that can make people sick, and they think it helps the fungus deal with harmful substances.
Methodology
The protein was expressed in E. coli, purified, and crystallized, with structures determined using X-ray crystallography.
Limitations
The actual enzymatic activity of the protein and its substrates remain to be determined.
Digital Object Identifier (DOI)
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