8A0R
Crystal structure of poplar glutathione transferase U20 in complex with pinocembrin
8A0R の概要
エントリーDOI | 10.2210/pdb8a0r/pdb |
関連するPDBエントリー | 7ZZN 8A08 8A0I 8A0O 8A0P 8A0Q |
分子名称 | Glutathione transferase, pinocembrin, CHLORIDE ION, ... (5 entities in total) |
機能のキーワード | glutathione, tau, transferase, plant |
由来する生物種 | Populus trichocarpa (black cottonwood) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 25371.82 |
構造登録者 | |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.6 Å) |
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