ArticleBioscience reports2015
Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site.
Article in Bioscience reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Structural and Thermodynamic Insights into Dimerization Interfaces of Drosophila Glutathione Transferases.Biomolecules · 2024Article
- Structural Analysis of theBiomolecules · 2024Article
- Conserved Residues Lys64 and Glu78 at the Subunit Surface of Tau Glutathione Transferase in Rice Affect Structure and Enzymatic Properties.International journal of molecular sciences · 2023Article
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- Gut transcriptome of two bark beetle species stimulated with the same kairomones reveals molecular differences in detoxification pathways.Computational and structural biotechnology journal · 2022Article
- Functional and Structural Diversity of Insect Glutathione S-transferases in Xenobiotic Adaptation.International journal of biological sciences · 2022Review
- Investigation of the active site of an unclassified glutathione transferase inJournal of pesticide science · 2020Article
- Anopheles metabolic proteins in malaria transmission, prevention and control: a review.Parasites & vectors · 2020Review
- RNA-sequencing analysis of fungi-induced transcripts from the bamboo wireworm Melanotus cribricollis (Coleoptera: Elateridae) larvae.PloS one · 2018Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Epsilon class glutathione transferases (GSTs) have been shown to contribute significantly to insecticide resistance. We report a new Epsilon class protein crystal structure from Drosophila melanogaster for the glutathione transferase DmGSTE6. The structure reveals a novel Epsilon clasp motif that is conserved across hundreds of millions of years of evolution of the insect Diptera order. This histidine-serine motif lies in the subunit interface and appears to contribute to quaternary stability as well as directly connecting the two glutathiones in the active sites of this dimeric enzyme.
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