3N5O

Crystal structure of putative glutathione transferase from Coccidioides immitis bound to glutathione

Summary for 3N5O

• Entry DOI: 10.2210/pdb3n5o/pdb
• Related: 3LG6
• Descriptor: glutathione transferase, GLUTATHIONE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: seattle structural genomics center for infectious disease, ssgcid, gst, glutathione, transferase, pathogenic fungus, coccidioidomycosis, valley fever, meningitis
• Biological source: Coccidioides immitis
• Total number of polymer chains: 2
• Total formula weight: 52422.81

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2010-05-25, release date: 2010-06-16, Last modification date: 2023-09-06)

Primary citation

Edwards, T.E.,Bryan, C.M.,Leibly, D.J.,Dieterich, S.H.,Abendroth, J.,Sankaran, B.,Sivam, D.,Staker, B.L.,Van Voorhis, W.C.,Myler, P.J.,Stewart, L.J.
Structures of a putative zeta-class glutathione S-transferase from the pathogenic fungus Coccidioides immitis.
Acta Crystallogr.,Sect.F, 67:1038-1043, 2011

PubMed Abstract: Coccidioides 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 ζ-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 ζ-class glutathione S-transferase, a maleylacetoacetate isomerase (MAAI).

PubMed: 21904047
DOI: 10.1107/S1744309111009493

Experimental method

X-RAY DIFFRACTION (1.85 Å)