ArticleThe EMBO journal1995
Crystal structure of a theta-class glutathione transferase.
Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed.
- Tyr76 is essential for the cold adaptation of a class II glutaredoxin 4 with a heat-labile structure from the Arctic bacterium Sphingomonas sp.FEBS open bio · 2023Article
- Structural and biochemical characterization of a glutathione transferase from the citrus canker pathogen Xanthomonas.Acta crystallographica. Section D, Structural biology · 2020Article
- Mechanisms of promiscuity among drug metabolizing enzymes and drug transporters.The FEBS journal · 2020Review
- Glutathione S-transferase is a good biomarker in acrylamide induced neurotoxicity and genotoxicity.Interdisciplinary toxicology · 2018Review
- Analyses of Genetic Variations of Glutathione S-Transferase Mu1 and Theta1 Genes in Bangladeshi Tannery Workers and Healthy Controls.BioMed research international · 2016Article
- Characterization of a Highly pH Stable Chi-Class Glutathione S-Transferase from Synechocystis PCC 6803.PloS one · 2015Article
- Expression of SbGSTU (tau class glutathione S-transferase) gene isolated from Salicornia brachiata in tobacco for salt tolerance.Molecular biology reports · 2011Article
- A functionally conserved basic residue in glutathione transferases interacts with the glycine moiety of glutathione and is pivotal for enzyme catalysis.The Biochemical journal · 2007Article
- Crystallization and preliminary X-ray crystallographic analysis of a highly stable mutant V107A of glutathione transferase from Anopheles dirus in complex with glutathione.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006Article
- The structural roles of a conserved small hydrophobic core in the active site and an ionic bridge in domain I of Delta class glutathione S-transferase.The Biochemical journal · 2006Article
- Catalytic and structural contributions for glutathione-binding residues in a Delta class glutathione S-transferase.The Biochemical journal · 2004Article
- Does glutathione S-transferase Pi (GST-Pi) a marker protein for cancer?Molecular and cellular biochemistry · 2003Review
- Clarification of the role of key active site residues of glutathione transferase zeta/maleylacetoacetate isomerase by a new spectrophotometric technique.The Biochemical journal · 2003Article
- Molecular cloning, expression and characterization of a novel class glutathione S-transferase from the fungus Cunninghamella elegans.The Biochemical journal · 2002Article
- A gene from Aspergillus nidulans with similarity to URE2 of Saccharomyces cerevisiae encodes a glutathione S-transferase which contributes to heavy metal and xenobiotic resistance.Applied and environmental microbiology · 2002Article
- Glutamic acid-65 is an essential residue for catalysis in Proteus mirabilis glutathione S-transferase B1-1.The Biochemical journal · 2002Article
- Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily.The Biochemical journal · 2001Review
- The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B.Protein science : a publication of the Protein Society · 2001Article
- Identification of a novel class of insect glutathione S-transferases involved in resistance to DDT in the malaria vector Anopheles gambiae.The Biochemical journal · 2001Article
- The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
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4 authors.
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Abstract
Glutathione S-transferases (GSTs) are a family of enzymes involved in the cellular detoxification of xenotoxins. Cytosolic GSTs have been grouped into four evolutionary classes for which there are representative crystal structures of three of them. Here we report the first crystal structure of a theta-class GST. So far, all available GST crystal structures suggest that a strictly conserved tyrosine near the N-terminus plays a critical role in the reaction mechanism and such a role has been convincingly demonstrated by site-directed mutagenesis. Surprisingly, the equivalent residue in the theta-class structure is not in the active site, but its role appears to have been replaced by either a nearby serine or by another tyrosine residue located in the C-terminal domain of the enzyme.
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