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https://doi.org/10.1042/BSR20150183
| Title: | Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site | Authors: | Wongsantichon, J Robinson, R.C Ketterman, A.J |
Keywords: | glutathione glutathione transferase glutathione transferase E6 histidine serine unclassified drug Drosophila protein glutathione glutathione transferase GSTE6 protein, Drosophila amino acid sequence Article binding affinity controlled study crystal structure Drosophila melanogaster enzyme specificity molecular interaction nonhuman protein folding protein quaternary structure protein subunit residue analysis sequence alignment sequence analysis structure activity relation structure analysis animal binding site chemistry enzyme active site enzymology genetics metabolism protein conformation protein motif X ray crystallography Amino Acid Motifs Amino Acid Sequence Animals Binding Sites Catalytic Domain Crystallography, X-Ray Drosophila melanogaster Drosophila Proteins Glutathione Glutathione Transferase Protein Conformation |
Issue Date: | 2015 | Publisher: | Portland Press Ltd | Citation: | Wongsantichon, J, Robinson, R.C, Ketterman, A.J (2015). Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site. Bioscience Reports 35 (6) : e00272. ScholarBank@NUS Repository. https://doi.org/10.1042/BSR20150183 | Rights: | Attribution 4.0 International | 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. © 2015 Authors. | Source Title: | Bioscience Reports | URI: | https://scholarbank.nus.edu.sg/handle/10635/179632 | ISSN: | 0144-8463 | DOI: | 10.1042/BSR20150183 | Rights: | Attribution 4.0 International |
| Appears in Collections: | Staff Publications Elements |
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