Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site

  • Wongsantichon J
  • Robinson R
  • Ketterman A
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Abstract

Synopsis 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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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–e00272. https://doi.org/10.1042/bsr20150183

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