Jantana WongsantichonRobert C. RobinsonAlbert J. KettermanInstitute of Molecular and Cell Biology, A-Star, SingaporeNational University of SingaporeMahidol University2018-11-232018-11-232015-12-01Bioscience Reports. Vol.35, No.6 (2015)15734935014484632-s2.0-84969389427https://repository.li.mahidol.ac.th/handle/123456789/35335© 2015 Authors. 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.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyArticleSCOPUS10.1042/BSR20150183