Structural characterization of the catalytic site of a Nilaparvata lugens delta-class glutathione transferase

Kohji Yamamoto, Akifumi Higashiura, Md Tofazzal Hossain, Naotaka Yamada, Takahiro Shiotsuki, Atsushi Nakagawa

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)

Abstract

Glutathione transferases (GSTs) are a major class of detoxification enzymes that play a central role in the defense against environmental toxicants and oxidative stress. Here, we studied the crystal structure of a delta-class glutathione transferase from Nilaparvata lugens, nlGSTD, to gain insights into its catalytic mechanism. The structure of nlGSTD in complex with glutathione, determined at a resolution of 1.7 Å, revealed that it exists as a dimer and its secondary and tertiary structures are similar to those of other delta-class GSTs. Analysis of a complex between nlGSTD and glutathione showed that the bound glutathione was localized to the glutathione-binding site. Site-directed mutagenesis of nlGSTD mutants indicated that amino acid residues Ser11, His52, Glu66, and Phe119 contribute to catalytic activity.

Original languageEnglish
Pages (from-to)36-42
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume566
DOIs
Publication statusPublished - Jan 15 2015

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Structural characterization of the catalytic site of a Nilaparvata lugens delta-class glutathione transferase'. Together they form a unique fingerprint.

Cite this