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

DOI: 10.1042/BSR20150183 DOI Help
PMID: 26487708 PMID Help

Authors: Jantana Wongsantichon (Institute of Molecular and Cell Biology) , R. C. Robinson (National University of Singapore) , A. J. Ketterman (Mahidol University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Bioscience Reports , VOL 35 , PAGES e00272 - e00272

State: Published (Approved)
Published: November 2015
Diamond Proposal Number(s): 8423

Open Access Open Access

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.

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography

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