PDBsum entry 6f67

Transferase

PDB id: 6f67

Contents

Protein chains

241 a.a.

Ligands

CUQ ×2

PEG ×2

Metals

_CA

Waters ×158

PDB id:

6f67

Name:

Transferase

Title:

Crystal structure of glutathione transferase omega 3s from trametes versicolor in complex with 3,4-dihydroxybenzophenone

Structure:

Glutathione transferase. Chain: a, b. Engineered: yes

Source:

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

Resolution:

2.40Å R-factor: 0.183 R-free: 0.201

Authors:

M.Schwartz,F.Favier,C.Didierjean

Key ref:

M.Schwartz et al. (2018). Molecular recognition of wood polyphenols by phase II detoxification enzymes of the white rot Trametes versicolor. Sci Rep, 8, 8472. PubMed id: 29855494

Date:

05-Dec-17 Release date: 06-Jun-18

Protein chains

A0A384E145  (A0A384E145_TRAVE) -  Glutathione transferase from Trametes versicolor

Seq: 246 a.a.

Struc: 241 a.a.

Enzyme reactions

• Enzyme class: E.C.2.5.1.18 - glutathione transferase.
• Reaction: RX + glutathione = an S-substituted glutathione + a halide anion + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

Sci Rep 8:8472 (2018)

PubMed id: 29855494

Molecular recognition of wood polyphenols by phase II detoxification enzymes of the white rot Trametes versicolor.

M.Schwartz, T.Perrot, E.Aubert, S.Dumarçay, F.Favier, P.Gérardin, M.Morel-Rouhier, G.Mulliert, F.Saiag, C.Didierjean, E.Gelhaye.

ABSTRACT

Wood decay fungi have complex detoxification systems that enable them to cope with secondary metabolites produced by plants. Although the number of genes encoding for glutathione transferases is especially expanded in lignolytic fungi, little is known about their target molecules. In this study, by combining biochemical, enzymatic and structural approaches, interactions between polyphenols and six glutathione transferases from the white-rot fungus Trametes versicolor have been demonstrated. Two isoforms, named TvGSTO3S and TvGSTO6S have been deeply studied at the structural level. Each isoform shows two distinct ligand-binding sites, a narrow L-site at the dimer interface and a peculiar deep hydrophobic H-site. In TvGSTO3S, the latter appears optimized for aromatic ligand binding such as hydroxybenzophenones. Affinity crystallography revealed that this H-site retains the flavonoid dihydrowogonin from a partially purified wild-cherry extract. Besides, TvGSTO6S binds two molecules of the flavonoid naringenin in the L-site. These data suggest that TvGSTO isoforms could interact with plant polyphenols released during wood degradation.