Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCoccidioides immitis is a pathogenic fungus populating the southwestern United States and is a causative agent of coccidioidomycosis, sometimes referred to as Valley Fever. Although the genome of this fungus has been sequenced, many operons are not properly annotated. Crystal structures are presented for a putative uncharacterized protein that shares sequence similarity with zeta-class glutathione S-transferases (GSTs) in both apo and glutathione-bound forms. The apo structure reveals a nonsymmetric homodimer with each protomer comprising two subdomains: a C-terminal helical domain and an N-terminal thioredoxin-like domain that is common to all GSTs. Half-site binding is observed in the glutathione-bound form. Considerable movement of some components of the active site relative to the glutathione-free form was observed, indicating an induced-fit mechanism for cofactor binding. The sequence homology, structure and half-site occupancy imply that the protein is a zeta-class glutathione S-transferase, a maleylacetoacetate isomerase (MAAI). Structures of a putative zeta-class glutathione S-transferase from the pathogenic fungus Coccidioides immitis.,Edwards TE, Bryan CM, Leibly DJ, Dieterich SH, Abendroth J, Sankaran B, Sivam D, Staker BL, Van Voorhis WC, Myler PJ, Stewart LJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1038-43. Epub 2011 Aug 13. PMID:21904047[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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