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 journalArticle

10 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

Fingerprint

Glutathione Transferase
Glutathione
Catalytic Domain
Detoxification
Mutagenesis
Oxidative stress
Site-Directed Mutagenesis
Dimers
Catalyst activity
Oxidative Stress
Crystal structure
Binding Sites
Amino Acids
Enzymes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

Structural characterization of the catalytic site of a Nilaparvata lugens delta-class glutathione transferase. / Yamamoto, Kohji; Higashiura, Akifumi; Hossain, Md Tofazzal; Yamada, Naotaka; Shiotsuki, Takahiro; Nakagawa, Atsushi.

In: Archives of Biochemistry and Biophysics, Vol. 566, 15.01.2015, p. 36-42.

Research output: Contribution to journalArticle

Yamamoto, Kohji ; Higashiura, Akifumi ; Hossain, Md Tofazzal ; Yamada, Naotaka ; Shiotsuki, Takahiro ; Nakagawa, Atsushi. / Structural characterization of the catalytic site of a Nilaparvata lugens delta-class glutathione transferase. In: Archives of Biochemistry and Biophysics. 2015 ; Vol. 566. pp. 36-42.
@article{5d785e9468204c81af4cdabca983b61f,
title = "Structural characterization of the catalytic site of a Nilaparvata lugens delta-class glutathione transferase",
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 {\AA}, 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.",
author = "Kohji Yamamoto and Akifumi Higashiura and Hossain, {Md Tofazzal} and Naotaka Yamada and Takahiro Shiotsuki and Atsushi Nakagawa",
year = "2015",
month = "1",
day = "15",
doi = "10.1016/j.abb.2014.12.001",
language = "English",
volume = "566",
pages = "36--42",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press Inc.",

}

TY - JOUR

T1 - Structural characterization of the catalytic site of a Nilaparvata lugens delta-class glutathione transferase

AU - Yamamoto, Kohji

AU - Higashiura, Akifumi

AU - Hossain, Md Tofazzal

AU - Yamada, Naotaka

AU - Shiotsuki, Takahiro

AU - Nakagawa, Atsushi

PY - 2015/1/15

Y1 - 2015/1/15

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84919897648&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84919897648&partnerID=8YFLogxK

U2 - 10.1016/j.abb.2014.12.001

DO - 10.1016/j.abb.2014.12.001

M3 - Article

C2 - 25497345

AN - SCOPUS:84919897648

VL - 566

SP - 36

EP - 42

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

ER -