6GCC

Crystal structure of glutathione transferase Xi 3 mutant C56S from Trametes versicolor in complex with dextran-sulfate

6GCC の概要

• エントリーDOI: 10.2210/pdb6gcc/pdb
• 分子名称: Glutathione transferase Xi 3 mutant C56S, 3,4-di-O-sulfo-alpha-D-glucopyranose-(1-6)-3,4-di-O-sulfo-alpha-D-altropyranose-(1-6)-1,2,3,4-tetra-O-sulfo-alpha-D-allopyranose (3 entities in total)
• 機能のキーワード: glutathione transferase, 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: 76584.05

構造登録者

Schwartz, M.,Favier, F.,Didierjean, C. (登録日: 2018-04-17, 公開日: 2018-08-29, 最終更新日: 2024-01-17)

主引用文献

Schwartz, M.,Perrot, T.,Deroy, A.,Roret, T.,Morel-Rouhier, M.,Mulliert, G.,Gelhaye, E.,Favier, F.,Didierjean, C.
Trametes versicolor glutathione transferase Xi 3, a dual Cys-GST with catalytic specificities of both Xi and Omega classes.
FEBS Lett., 592:3163-3172, 2018

PubMed Abstract: Glutathione transferases (GSTs) from the Xi and Omega classes have a catalytic cysteine residue, which gives them reductase activities. Until now, they have been assigned distinct substrates. While Xi GSTs specifically reduce glutathionyl-(hydro)quinones, Omega GSTs are specialized in the reduction of glutathionyl-acetophenones. Here, we present the biochemical and structural analysis of TvGSTX1 and TvGSTX3 isoforms from the wood-degrading fungus Trametes versicolor. TvGSTX1 reduces GS-menadione as expected, while TvGSTX3 reduces both Xi and Omega substrates. An in-depth structural analysis indicates a broader active site for TvGSTX3 due to specific differences in the nature of the residues situated in the C-terminal helix α9. This feature could explain the catalytic duality of TvGSTX3. Based on phylogenetic analysis, we propose that this duality might exist in saprophytic fungi and ascomycetes.

PubMed: 30112765
DOI: 10.1002/1873-3468.13224

実験手法

X-RAY DIFFRACTION (1.9 Å)