6W1G
Crystal structure of the hydroxyglutarate synthase from Pseudomonas putida
6W1G の概要
| エントリーDOI | 10.2210/pdb6w1g/pdb |
| 分子名称 | Hydroxyglutarate synthase, NICKEL (II) ION (3 entities in total) |
| 機能のキーワード | decarboxylase lysine catabolism, lyase |
| 由来する生物種 | Pseudomonas putida |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 51486.50 |
| 構造登録者 | Pereira, J.H.,Thompson, M.G.,Blake-Hedges, J.M.,Keasling, J.D.,Adams, P.D. (登録日: 2020-03-04, 公開日: 2020-06-24, 最終更新日: 2023-10-18) |
| 主引用文献 | Thompson, M.G.,Blake-Hedges, J.M.,Pereira, J.H.,Hangasky, J.A.,Belcher, M.S.,Moore, W.M.,Barajas, J.F.,Cruz-Morales, P.,Washington, L.J.,Haushalter, R.W.,Eiben, C.B.,Liu, Y.,Skyrud, W.,Benites, V.T.,Barnum, T.P.,Baidoo, E.E.K.,Scheller, H.V.,Marletta, M.A.,Shih, P.M.,Adams, P.D.,Keasling, J.D. An iron (II) dependent oxygenase performs the last missing step of plant lysine catabolism. Nat Commun, 11:2931-2931, 2020 Cited by PubMed Abstract: Despite intensive study, plant lysine catabolism beyond the 2-oxoadipate (2OA) intermediate remains unvalidated. Recently we described a missing step in the D-lysine catabolism of Pseudomonas putida in which 2OA is converted to D-2-hydroxyglutarate (2HG) via hydroxyglutarate synthase (HglS), a DUF1338 family protein. Here we solve the structure of HglS to 1.1 Å resolution in substrate-free form and in complex with 2OA. We propose a successive decarboxylation and intramolecular hydroxylation mechanism forming 2HG in a Fe(II)- and O-dependent manner. Specificity is mediated by a single arginine, highly conserved across most DUF1338 proteins. An Arabidopsis thaliana HglS homolog coexpresses with known lysine catabolism enzymes, and mutants show phenotypes consistent with disrupted lysine catabolism. Structural and biochemical analysis of Oryza sativa homolog FLO7 reveals identical activity to HglS despite low sequence identity. Our results suggest DUF1338-containing enzymes catalyze the same biochemical reaction, exerting the same physiological function across bacteria and eukaryotes. PubMed: 32523014DOI: 10.1038/s41467-020-16815-3 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.14 Å) |
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