3S61
Reduced Form of Ornithine Hydroxylase (PvdA) from Pseudomonas aeruginosa
3S61 の概要
| エントリーDOI | 10.2210/pdb3s61/pdb |
| 関連するPDBエントリー | 3S5W |
| 分子名称 | L-ornithine 5-monooxygenase, FLAVIN-ADENINE DINUCLEOTIDE, L-ornithine, ... (4 entities in total) |
| 機能のキーワード | n5-l-ornithine monooxygenase, reduced form, class b flavin dependent n-hydroxylating monooxygenase, ornithine hydroxylase, bacterial cytosol, oxidoreductase |
| 由来する生物種 | Pseudomonas aeruginosa |
| 細胞内の位置 | Cell inner membrane ; Peripheral membrane protein ; Cytoplasmic side : Q51548 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 106748.59 |
| 構造登録者 | |
| 主引用文献 | Olucha, J.,Meneely, K.M.,Chilton, A.S.,Lamb, A.L. Two Structures of an N-Hydroxylating Flavoprotein Monooxygenase: ORNITHINE HYDROXYLASE FROM PSEUDOMONAS AERUGINOSA. J.Biol.Chem., 286:31789-31798, 2011 Cited by PubMed Abstract: The ornithine hydroxylase from Pseudomonas aeruginosa (PvdA) catalyzes the FAD-dependent hydroxylation of the side chain amine of ornithine, which is subsequently formylated to generate the iron-chelating hydroxamates of the siderophore pyoverdin. PvdA belongs to the class B flavoprotein monooxygenases, which catalyze the oxidation of substrates using NADPH as the electron donor and molecular oxygen. Class B enzymes include the well studied flavin-containing monooxygenases and Baeyer-Villiger monooxygenases. The first two structures of a class B N-hydroxylating monooxygenase were determined with FAD in oxidized (1.9 Å resolution) and reduced (3.03 Å resolution) states. PvdA has the two expected Rossmann-like dinucleotide-binding domains for FAD and NADPH and also a substrate-binding domain, with the active site at the interface between the three domains. The structures have NADP(H) and (hydroxy)ornithine bound in a solvent-exposed active site, providing structural evidence for substrate and co-substrate specificity and the inability of PvdA to bind FAD tightly. Structural and biochemical evidence indicates that NADP(+) remains bound throughout the oxidative half-reaction, which is proposed to shelter the flavin intermediates from solvent and thereby prevent uncoupling of NADPH oxidation from hydroxylated product formation. PubMed: 21757711DOI: 10.1074/jbc.M111.265876 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.03 Å) |
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