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

Jantana Wongsantichon | Zendy; Robert Robinson | Zendy; Albert J. Ketterman | Zendy

Open Access

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 Robinson,

Albert J. Ketterman

Publication year - 2015

Publication title -

bioscience reports

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.938

H-Index - 77

eISSN - 1573-4935

pISSN - 0144-8463

DOI - 10.1042/bsr20150183

Subject(s) - protein subunit , active site , drosophila melanogaster , glutathione , serine , biology , protein quaternary structure , glutathione s transferase , histidine , conserved sequence , glutathione transferase , biochemistry , enzyme , transferase , genetics , peptide sequence , gene

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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