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• W2311502593 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." @default.
• W2311502593 created "2016-06-24" @default.
• W2311502593 creator A5043403706 @default.
• W2311502593 creator A5065591601 @default.
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• W2311502593 date "2015-11-26" @default.
• W2311502593 modified "2023-10-05" @default.
• W2311502593 title "Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site" @default.
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• W2311502593 doi "https://doi.org/10.1042/bsr20150183" @default.
• W2311502593 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4660579" @default.
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• W2311502593 hasPublicationYear "2015" @default.
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