6F68

Crystal structure glutathione transferase Omega 3S from Trametes versicolor in complex with 2,4,4'-trihydroxybenzophenone

6F68 の概要

• エントリーDOI: 10.2210/pdb6f68/pdb
• 関連するPDBエントリー: 6F43 6F4B 6F4F 6F4K 6F51 6F66 6F67
• 分子名称: glutathione transferase, (2,4-dihydroxyphenyl)(4-hydroxyphenyl)methanone, GLUTATHIONE, ... (8 entities in total)
• 機能のキーワード: glutathione, fungi, polyphenols, wood decayers, 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: 56652.70

構造登録者

Schwartz, M.,Favier, F.,Didierjean, C. (登録日: 2017-12-05, 公開日: 2018-06-06, 最終更新日: 2024-01-17)

主引用文献

Schwartz, M.,Perrot, T.,Aubert, E.,Dumarcay, S.,Favier, F.,Gerardin, P.,Morel-Rouhier, M.,Mulliert, G.,Saiag, F.,Didierjean, C.,Gelhaye, E.
Molecular recognition of wood polyphenols by phase II detoxification enzymes of the white rot Trametes versicolor.
Sci Rep, 8:8472-8472, 2018

PubMed 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.

PubMed: 29855494
DOI: 10.1038/s41598-018-26601-3

実験手法

X-RAY DIFFRACTION (1.696 Å)