6F68
Crystal structure glutathione transferase Omega 3S from Trametes versicolor in complex with 2,4,4'-trihydroxybenzophenone
Summary for 6F68
| Entry DOI | 10.2210/pdb6f68/pdb |
| Related | 6F43 6F4B 6F4F 6F4K 6F51 6F66 6F67 |
| Descriptor | glutathione transferase, (2,4-dihydroxyphenyl)(4-hydroxyphenyl)methanone, GLUTATHIONE, ... (8 entities in total) |
| Functional Keywords | glutathione, fungi, polyphenols, wood decayers, transferase |
| Biological source | Trametes versicolor |
| Total number of polymer chains | 2 |
| Total formula weight | 56652.70 |
| Authors | Schwartz, M.,Favier, F.,Didierjean, C. (deposition date: 2017-12-05, release date: 2018-06-06, Last modification date: 2024-01-17) |
| Primary citation | 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 Cited by 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: 29855494DOI: 10.1038/s41598-018-26601-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.696 Å) |
Structure validation
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