7OPY

Camel GSTM1-1 in complex with S-(p-nitrobenzyl)glutathione

7OPY の概要

• エントリーDOI: 10.2210/pdb7opy/pdb
• 分子名称: Glutathione transferase, S-(P-NITROBENZYL)GLUTATHIONE, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: glutathione, detoxification, pesticides, adaptation, transferase
• 由来する生物種: Camelus dromedarius (Arabian camel)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 105123.27

構造登録者

Papageorgiou, A.C.,Poudel, N. (登録日: 2021-06-02, 公開日: 2022-02-16, 最終更新日: 2024-10-23)

主引用文献

Perperopoulou, F.,Poudel, N.,Papageorgiou, A.C.,Ataya, F.S.,Labrou, N.E.
Structural and Functional Characterization of Camelus dromedarius Glutathione Transferase M1-1.
Life, 12:-, 2022

PubMed Abstract: Glutathione transferases (GSTs; EC. 2.5.1.18) are a large family of multifunctional enzymes that play crucial roles in the metabolism and inactivation of a broad range of xenobiotic compounds. In the present work, we report the kinetic and structural characterization of the isoenzyme GSTM1-1 from (GSTM1-1). The GSΤM1-1 was expressed in BL21 (DE3) and was purified by affinity chromatography. Kinetics analysis showed that the enzyme displays a relative narrow substrate specificity and restricted ability to bind xenobiotic compounds. The crystal structures of GSΤM1-1 were determined by X-ray crystallography in complex with the substrate (GSH) or the reaction product (S-p-nitrobenzyl-GSH), providing snapshots of the induced-fit catalytic mechanism. The thermodynamic stability of GSTM1-1 was investigated using differential scanning fluorimetry (DSF) in the absence and in presence of GSH and S-p-nitrobenzyl-GSH and revealed that the enzyme's structure is significantly stabilized by its ligands. The results of the present study advance the understanding of camelid GST detoxification mechanisms and their contribution to abiotic stress adaptation in harsh desert conditions.

PubMed: 35054499
DOI: 10.3390/life12010106

実験手法

X-RAY DIFFRACTION (2.05 Å)