2VE3
Retinoic acid bound cyanobacterial CYP120A1
2VE3 の概要
| エントリーDOI | 10.2210/pdb2ve3/pdb |
| 関連するPDBエントリー | 2VE4 |
| 分子名称 | PUTATIVE CYTOCHROME P450 120, PROTOPORPHYRIN IX CONTAINING FE, RETINOIC ACID, ... (4 entities in total) |
| 機能のキーワード | oxidoreductase, monooxygenase, metal-binding, heme, iron |
| 由来する生物種 | SYNECHOCYSTIS SP. |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 103100.10 |
| 構造登録者 | Kuhnel, K.,Ke, N.,Sligar, S.G.,Schuler, M.A.,Schlichting, I. (登録日: 2007-10-15, 公開日: 2008-04-29, 最終更新日: 2024-05-01) |
| 主引用文献 | Kuhnel, K.,Ke, N.,Cryle, M.J.,Sligar, S.G.,Schuler, M.A.,Schlichting, I. Crystal Structures of Substrate-Free and Retinoic Acid-Bound Cyanobacterial Cytochrome P450 Cyp120A1. Biochemistry, 47:6552-, 2008 Cited by PubMed Abstract: The crystal structures of substrate-free and all-trans-retinoic acid-bound CYP120A1 from Synechocystis sp. PCC 6803 were determined at 2.4 and 2.1 A resolution, respectively, representing the first structural characterization of a cyanobacterial P450. Features of CYP120A1 not observed in other P450 structures include an aromatic ladder flanking the channel leading to the active site and a triple-glycine motif within SRS5. Using spectroscopic methods, CYP120A1 is shown to bind 13-cis-retinoic acid, 9-cis-retinoic acid, and retinal with high affinity and dissociation constants of less than 1 microM. Metabolism of retinoic acid by CYP120A1 suggests that CYP120A1 hydroxylates a variety of retinoid derivatives in vivo. On the basis of the retinoic acid-bound CYP120A1 crystal structure, we propose that either carbon 2 or the methyl groups (C16 or C17) of the beta-ionone ring are modified by CYP120A1. PubMed: 18512957DOI: 10.1021/BI800328S 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.1 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






