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

研究成果: Contribution to journalArticle査読

13 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)36-42
ページ数7
ジャーナルArchives of Biochemistry and Biophysics
566
DOI
出版ステータス出版済み - 1 15 2015

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 生化学
  • 分子生物学

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