6J3E

Crystal structure of an apo form of the glutathione S-transferase, CsGST63524, of Ceriporiopsis subvermispora

6J3E の概要

• エントリーDOI: 10.2210/pdb6j3e/pdb
• 分子名称: glutathione S-transferase, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: glutathione s-transferase, ceriporiopsis subvermispora, transferase
• 由来する生物種: Ceriporiopsis subvermispora (strain B) (White-rot fungus)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58395.94

構造登録者

Osman, W.H.W.,Mikami, B.,Saka, N.,Kondo, K.,Nagata, T.,Katahira, M. (登録日: 2019-01-04, 公開日: 2019-02-27, 最終更新日: 2023-11-22)

主引用文献

Osman, W.H.W.,Mikami, B.,Saka, N.,Kondo, K.,Nagata, T.,Katahira, M.
Structure of a serine-type glutathione S-transferase of Ceriporiopsis subvermispora and identification of the enzymatically important non-canonical residues by functional mutagenesis.
Biochem. Biophys. Res. Commun., 510:177-183, 2019

PubMed Abstract: Ceriporiopsis subvermispora (C. subvermispora), one of the white-rot fungi, is known as a selective lignin degrader of the woody biomass. Glutathione S-transferases (GSTs) are multifunctional enzymes that are capable of catalyzing the reactions involved in detoxification and metabolic pathways. In this study, a GST of C. subvermispora, named CsGST63524, was overexpressed in E. coli, and then purified by affinity, anion exchange, and size exclusion column chromatography. The crystal structures of the CsGST63524 in ligand-free and complex with GSH were refined at 2.45 and 2.50 Å resolutions, respectively. The sulfur atom of glutathione forms a hydrogen bond with Ser21 of CsGST63524, indicating it is a serine-type GST. Mutagenesis of Ser21 unexpectedly indicated that this serine residue is not essential for the enzymatic activity of CsGST63524. Comparative sequence and structural analyses, together with functional mutagenesis, newly identified the enzymatically important non-canonical amino acid residues, Asn23 and Tyr45, other than the serine residue.

PubMed: 30683313
DOI: 10.1016/j.bbrc.2019.01.076

実験手法

X-RAY DIFFRACTION (2.455 Å)