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

doi:10.1016/j.abb.2014.12.001

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Article

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

Archives of biochemistry and biophysics - 15 Jan 2015

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

Abstract excerpt

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 insigh...

Topics

Amino Acid Sequence
Animals
Catalytic Domain
Crystallography, X-Ray
Escherichia coli
Gene Expression
Glutathione
Glutathione Transferase
Hemiptera
Insect Proteins
Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutation

Protein Binding

Protein Structure, Secondary

Recombinant Proteins

Sequence Alignment

Structure-Activity Relationship

Source

Open in PubMed

Identifiers

PMID: 25497345
DOI: 10.1016/j.abb.2014.12.001

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-25497345-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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