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

Jantana Wongsantichon, Robert C. Robinson, Albert J. Ketterman

Research output: Contribution to journalArticle

2 Citations (Scopus)

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.

Original languageEnglish
Article numbere00272
JournalBioscience Reports
Volume35
Issue number6
DOIs
Publication statusPublished - Dec 1 2015
Externally publishedYes

Fingerprint

Glutathione Transferase
Glutathione
Catalytic Domain
Insecticide Resistance
Insecticides
Drosophila melanogaster
Histidine
Diptera
Serine
Insects
Crystal structure
Enzymes
Proteins

Keywords

  • Dimer interface
  • Epsilon crystal structure
  • Gste6
  • Insect glutathione transferase
  • Protein structure

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site. / Wongsantichon, Jantana; Robinson, Robert C.; Ketterman, Albert J.

In: Bioscience Reports, Vol. 35, No. 6, e00272, 01.12.2015.

Research output: Contribution to journalArticle

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