8AX2

Crystal structure of Trametes versicolor glutathione transferase Omega 3S in complex with glutathione and pentachloro-nitrosyl-osmate

8AX2 の概要

• エントリーDOI: 10.2210/pdb8ax2/pdb
• 分子名称: Glutathione transferase, OSMIUM ION, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: glutathione transferase, gsto, detoxification, transferase
• 由来する生物種: Trametes versicolor
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56272.38

構造登録者

Schwartz, M.,Didierjean, C. (登録日: 2022-08-30, 公開日: 2023-03-01, 最終更新日: 2024-06-19)

主引用文献

Schwartz, M.,Perrot, T.,Beurton, J.,Zannini, F.,Morel-Rouhier, M.,Gelhaye, E.,Neiers, F.,Schaniel, D.,Favier, F.,Jacquot, J.P.,Leroy, P.,Clarot, I.,Boudier, A.,Didierjean, C.
Structural insights into the interactions of glutathione transferases with a nitric oxide carrier and sodium nitroprusside.
Biochem.Biophys.Res.Commun., 649:79-86, 2023

PubMed Abstract: Glutathione transferases are detoxification enzymes with multifaceted roles, including a role in the metabolism and scavenging of nitric oxide (NO) compounds in cells. Here, we explored the ability of Trametes versicolor glutathione transferases (GSTs) from the Omega class (TvGSTOs) to bind metal-nitrosyl compounds. TvGSTOs have been studied previously for their ligandin role and are interesting models to study protein‒ligand interactions. First, we determined the X-ray structure of the TvGSTO3S isoform bound to the dinitrosyl glutathionyl iron complex (DNGIC), a physiological compound involved in the storage of nitric oxide. Our results suggested a different binding mode compared to the one previously described in human GST Pi 1 (GSTP1). Then, we investigated the manner in which TvGSTO3S binds three nonphysiological metal-nitrosyl compounds with different metal cores (iron, ruthenium and osmium). We assayed sodium nitroprusside, a well-studied vasodilator used in cases of hypertensive crises or heart failure. Our results showed that the tested GST can bind metal-nitrosyls at two distinct binding sites. Thermal shift analysis with six isoforms of TvGSTOs identified TvGSTO6S as the best interactant. Using the Griess method, TvGSTO6S was found to improve the release of nitric oxide from sodium nitroprusside in vitro, whereas the effects of human GST alpha 1 (GSTA1) and GSTP1 were moderate. Our results open new structural perspectives for understanding the interactions of glutathione transferases with metal-nitrosyl compounds associated with the biochemical mechanisms of NO uptake/release in biological systems.

PubMed: 36758482
DOI: 10.1016/j.bbrc.2023.01.099

実験手法

X-RAY DIFFRACTION (1.62 Å)