1N5S
Crystal structure of a Monooxygenase from the gene ActVA-Orf6 of Streptomyces coelicolor in complex with the ligand Acetyl Dithranol
1N5S の概要
エントリーDOI | 10.2210/pdb1n5s/pdb |
関連するPDBエントリー | 1LQ9 1N5Q 1N5T 1N5V |
分子名称 | ActVA-Orf6 monooxygenase, 2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL, (1,8-DIHYDROXY-9-OXO-9,10-DIHYDRO-ANTHRACEN-2-YL)-ACETIC ACID, ... (4 entities in total) |
機能のキーワード | monooxygenase, aromatic polyketides, actinorhodin, dihydrokalafungin, acetyl dithranol, streptomyces coelicolor, oxidoreductase |
由来する生物種 | Streptomyces coelicolor |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 24493.41 |
構造登録者 | Sciara, G.,Kendrew, S.G.,Miele, A.E.,Marsh, N.G.,Federici, L.,Malatesta, F.,Schimperna, G.,Savino, C.,Vallone, B. (登録日: 2002-11-07, 公開日: 2003-01-14, 最終更新日: 2024-02-14) |
主引用文献 | Sciara, G.,Kendrew, S.G.,Miele, A.E.,Marsh, N.G.,Federici, L.,Malatesta, F.,Schimperna, G.,Savino, C.,Vallone, B. The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis Embo J., 22:205-215, 2003 Cited by PubMed Abstract: ActVA-Orf6 monooxygenase from Streptomyces coelicolor that catalyses the oxidation of an aromatic intermediate of the actinorhodin biosynthetic pathway is a member of a class of small monooxygenases that carry out oxygenation without the assistance of any of the prosthetic groups, metal ions or cofactors normally associated with activation of molecular oxygen. The overall structure is a ferredoxin-like fold with a novel dimeric assembly, indicating that the widely represented ferredoxin fold may sustain yet another functionality. The resolution (1.3 A) of the enzyme structure and its complex with substrate and product analogues allows us to visualize the mechanism of binding and activation of the substrate for attack by molecular oxygen, and utilization of two gates for the reaction components including a proton gate and an O(2)/H(2)O gate with a putative protein channel. This is the first crystal structure of an enzyme involved in the tailoring of a type II aromatic polyketide and illustrates some of the enzyme-substrate recognition features that may apply to a range of other enzymes involved in modifying a polyketide core structure. PubMed: 12514126DOI: 10.1093/emboj/cdg031 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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