ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011
Structures of a putative ζ-class glutathione S-transferase from the pathogenic fungus Coccidioides immitis.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 5 citations in OpenAlex.
- Observing How Glutathione and S-Hexyl Glutathione Bind to Glutathione S-Transferase fromInternational journal of molecular sciences · 2022Article
- Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases.Frontiers in plant science · 2019Review
- The impact of nitric oxide toxicity on the evolution of the glutathione transferase superfamily: a proposal for an evolutionary driving force.The Journal of biological chemistry · 2013Article
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Authors and funding
11 authors at 4 institutions in 1 country.
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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).
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