8A0P
Crystal structure of poplar glutathione transferase U20 in complex with morin
Summary for 8A0P
| Entry DOI | 10.2210/pdb8a0p/pdb |
| Related | 7ZZN 8A08 8A0I 8A0O |
| Descriptor | Glutathione transferase, CHLORIDE ION, 2-[2,4-bis(oxidanyl)phenyl]-3,5,7-tris(oxidanyl)chromen-4-one, ... (4 entities in total) |
| Functional Keywords | glutathione, tau, transferase, plant |
| Biological source | Populus trichocarpa (black cottonwood) |
| Total number of polymer chains | 1 |
| Total formula weight | 25331.11 |
| Authors | Didierjean, C.,Favier, F. (deposition date: 2022-05-30, release date: 2022-07-20, Last modification date: 2024-01-31) |
| Primary citation | Sylvestre-Gonon, E.,Morette, L.,Viloria, M.,Mathiot, S.,Boutilliat, A.,Favier, F.,Rouhier, N.,Didierjean, C.,Hecker, A. Biochemical and Structural Insights on the Poplar Tau Glutathione Transferase GSTU19 and 20 Paralogs Binding Flavonoids. Front Mol Biosci, 9:958586-958586, 2022 Cited by PubMed Abstract: Glutathione transferases (GSTs) constitute a widespread superfamily of enzymes notably involved in xenobiotic detoxification and/or in specialized metabolism. genome (V4.1 assembly, Phytozome 13) consists of 74 genes coding for full-length GSTs and ten likely pseudogenes. These GSTs are divided into 11 classes, in which the tau class (GSTU) is the most abundant with 54 isoforms. PtGSTU19 and 20, two paralogs sharing more than 91% sequence identity (95% of sequence similarity), would have diverged from a common ancestor of and species. These enzymes display the distinctive glutathione (GSH)-conjugation and peroxidase activities against model substrates. The resolution of the crystal structures of these proteins revealed significant structural differences despite their high sequence identity. PtGSTU20 has a well-defined deep pocket in the active site whereas the bottom of this pocket is disordered in PtGSTU19. In a screen of potential ligands, we were able to identify an interaction with flavonoids. Some of them, previously identified in poplar (chrysin, galangin, and pinocembrin), inhibited GSH-conjugation activity of both enzymes with a more pronounced effect on PtGSTU20. The crystal structures of PtGSTU20 complexed with these molecules provide evidence for their potential involvement in flavonoid transport in . PubMed: 36032685DOI: 10.3389/fmolb.2022.958586 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.686 Å) |
Structure validation
Download full validation report
