Structural highlights
Publication Abstract from PubMed
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.
Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site.,Wongsantichon J, Robinson RC, Ketterman AJ Biosci Rep. 2015 Oct 20;35(6). pii: e00272. doi: 10.1042/BSR20150183. PMID:26487708[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wongsantichon J, Robinson RC, Ketterman AJ. Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site. Biosci Rep. 2015 Oct 20;35(6). pii: e00272. doi: 10.1042/BSR20150183. PMID:26487708 doi:http://dx.doi.org/10.1042/BSR20150183
