PDBsum entry 6gcc

Transferase

PDB id: 6gcc

Contents

Protein chains

291 a.a.

Ligands

TUJ-TUG-5LT ×2

Waters ×732

PDB id:

6gcc

Name:

Transferase

Title:

Crystal structure of glutathione transferase xi 3 mutant c56s from trametes versicolor in complex with dextran-sulfate

Structure:

Glutathione transferase xi 3 mutant c56s. Chain: a, b. Engineered: yes

Source:

Trametes versicolor. Organism_taxid: 5325. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.90Å R-factor: 0.162 R-free: 0.193

Authors:

M.Schwartz,F.Favier,C.Didierjean

Key ref:

M.Schwartz et al. (2018). Trametes versicolor glutathione transferase Xi 3, a dual Cys-GST with catalytic specificities of both Xi and Omega classes. FEBS Lett, 592, 3163-3172. PubMed id: 30112765 DOI: 10.1002/1873-3468.13224

Date:

17-Apr-18 Release date: 29-Aug-18

Protein chains

A0A3F2YM29  (A0A3F2YM29_TRAVE) -  Glutathione transferase Xi 3 mutant C56S from Trametes versicolor

Seq: 325 a.a.

Struc: 291 a.a.

DOI no: 10.1002/1873-3468.13224

FEBS Lett 592:3163-3172 (2018)

PubMed id: 30112765

Trametes versicolor glutathione transferase Xi 3, a dual Cys-GST with catalytic specificities of both Xi and Omega classes.

M.Schwartz, T.Perrot, A.Deroy, T.Roret, M.Morel-Rouhier, G.Mulliert, E.Gelhaye, F.Favier, C.Didierjean.

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.