Unknown

Dataset Information

0

Structures of a putative ?-class glutathione S-transferase from the pathogenic fungus Coccidioides immitis.


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 ?-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 ?-class glutathione S-transferase, a maleylacetoacetate isomerase (MAAI).

SUBMITTER: Edwards TE 

PROVIDER: S-EPMC3169399 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structures of a putative ζ-class glutathione S-transferase from the pathogenic fungus Coccidioides immitis.

Edwards Thomas E TE   Bryan Cassie M CM   Leibly David J DJ   Dieterich Shellie H SH   Abendroth Jan J   Sankaran Banumathi B   Sivam Dhileep D   Staker Bart L BL   Van Voorhis Wesley C WC   Myler Peter J PJ   Stewart Lance J LJ  

Acta crystallographica. Section F, Structural biology and crystallization communications 20110813 Pt 9


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 nonsymmetri  ...[more]

Similar Datasets

| S-EPMC24704 | biostudies-literature
| S-EPMC2144563 | biostudies-other
| S-EPMC3212906 | biostudies-literature
| S-EPMC5029449 | biostudies-literature
| PRJNA820037 | ENA
| PRJNA12821 | ENA
| PRJNA245906 | ENA
| S-EPMC8496281 | biostudies-literature
| S-EPMC4029803 | biostudies-literature
| S-EPMC2658098 | biostudies-literature