ArticleEMBO reports2009
Structures of yeast glutathione-S-transferase Gtt2 reveal a new catalytic type of GST family.
Article in EMBO reports, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 33 citations in OpenAlex.
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- Biochemical and Structural Characterization of Chi-Class Glutathione Transferases: A Snapshot on the Glutathione Transferase Encoded byBiomolecules · 2022Article
- Whole Genome Sequencing and RNA-seq-Driven Discovery of New Targets That Affect Carotenoid Synthesis inFrontiers in microbiology · 2022Article
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- Structural and Mechanistic Insights into C-S Bond Formation in Gliotoxin.Angewandte Chemie (International ed. in English) · 2021Article
- FzlA, an essential regulator of FtsZ filament curvature, controls constriction rate during Caulobacter division.Molecular microbiology · 2018Article
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- Glutathione S-Transferase Gene Family in Gossypium raimondii and G. arboreum: Comparative Genomic Study and their Expression under Salt Stress.Frontiers in plant science · 2016Article
- Antioxidant enzymes activities of Burkholderia spp. strains-oxidative responses to Ni toxicity.Environmental science and pollution research international · 2015Article
- Transcriptomic responses of Phanerochaete chrysosporium to oak acetonic extracts: focus on a new glutathione transferase.Applied and environmental microbiology · 2014Article
- Mechanisms of tolerance and high degradation capacity of the herbicide mesotrione by Escherichia coli strain DH5-α.PloS one · 2014Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glutathione-S-transferases (GSTs) are ubiquitous detoxification enzymes that catalyse the conjugation of electrophilic substrates to glutathione. Here, we present the crystal structures of Gtt2, a GST of Saccharomyces cerevisiae, in apo and two ligand-bound forms, at 2.23 A, 2.20 A and 2.10 A, respectively. Although Gtt2 has the overall structure of a GST, the absence of the classic catalytic essential residues--tyrosine, serine and cysteine--distinguishes it from all other cytosolic GSTs of known structure. Site-directed mutagenesis in combination with activity assays showed that instead of the classic catalytic residues, a water molecule stabilized by Ser129 and His123 acts as the deprotonator of the glutathione sulphur atom. Furthermore, only glycine and alanine are allowed at the amino-terminus of helix-alpha1 because of stereo-hindrance. Taken together, these results show that yeast Gtt2 is a novel atypical type of cytosolic GST.
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