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

Issued Date

2015-12-01

Resource Type

Article

ISSN

15734935
01448463

DOI

10.1042/BSR20150183

Other identifier(s)

2-s2.0-84969389427

Rights

Mahidol University

Rights Holder(s)

SCOPUS

Bibliographic Citation

Bioscience Reports. Vol.35, No.6 (2015)

Suggested Citation

Jantana Wongsantichon, Robert C. Robinson, Albert J. Ketterman Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site. Bioscience Reports. Vol.35, No.6 (2015). doi:10.1042/BSR20150183 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/35335

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Title

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

Author(s)

Jantana Wongsantichon
 Robert C. Robinson
 Albert J. Ketterman

Other Contributor(s)

Institute of Molecular and Cell Biology, A-Star, Singapore
 National University of Singapore
 Mahidol University

Abstract

© 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.

Keyword(s)

Biochemistry, Genetics and Molecular Biology

Availability

URI

https://repository.li.mahidol.ac.th/handle/123456789/35335

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Scopus 2011-2015