3DBM

Crystal Structure of Allene oxide synthase

3DBM の概要

• エントリーDOI: 10.2210/pdb3dbm/pdb
• 関連するPDBエントリー: 3DAM 3DAN
• 分子名称: Cytochrome P450 74A2, PROTOPORPHYRIN IX CONTAINING FE, (9E,11E,13S)-13-hydroxyoctadeca-9,11-dienoic acid, ... (4 entities in total)
• 機能のキーワード: crystal structure hem hode aos, fatty acid biosynthesis, heme, iron, lipid synthesis, metal-binding, oxylipin biosynthesis, lyase
• 由来する生物種: Parthenium argentatum (Guayule rubber plant)
• 細胞内の位置: Note=Rubber particle: Q40778
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54445.91

構造登録者

Li, L.,Wang, X. (登録日: 2008-06-01, 公開日: 2008-09-23, 最終更新日: 2023-08-30)

主引用文献

Li, L.,Chang, Z.,Pan, Z.,Fu, Z.Q.,Wang, X.
Modes of heme binding and substrate access for cytochrome P450 CYP74A revealed by crystal structures of allene oxide synthase.
Proc.Natl.Acad.Sci.Usa, 105:13883-13888, 2008

PubMed Abstract: Cytochrome P450s exist ubiquitously in all organisms and are involved in many biological processes. Allene oxide synthase (AOS) is a P450 enzyme that plays a key role in the biosynthesis of oxylipin jasmonates, which are involved in signal and defense reactions in higher plants. The crystal structures of guayule (Parthenium argentatum) AOS (CYP74A2) and its complex with the substrate analog 13(S)-hydroxyoctadeca-9Z,11E-dienoic acid have been determined. The structures exhibit a classic P450 fold but possess a heme-binding mode with an unusually long heme binding loop and a unique I-helix. The structures also reveal two channels through which substrate and product may access and leave the active site. The entrances are defined by a loop between beta3-2 and beta3-3. Asn-276 in the substrate binding site may interact with the substrate's hydroperoxy group and play an important role in catalysis, and Lys-282 at the entrance may control substrate access and binding. These studies provide both structural insights into AOS and related P450s and a structural basis to understand the distinct reaction mechanism.

PubMed: 18787124
DOI: 10.1073/pnas.0804099105

実験手法

X-RAY DIFFRACTION (2.6 Å)