5MNS

Structural and functional characterization of OleP in complex with 6DEB in sodium formate

5MNS の概要

• エントリーDOI: 10.2210/pdb5mns/pdb
• 分子名称: Cytochrome P-450, PROTOPORPHYRIN IX CONTAINING FE, 6-DEOXYERYTHRONOLIDE B, ... (4 entities in total)
• 機能のキーワード: p450, cytochrome, 6deb, epoxidase, oxidoreductase
• 由来する生物種: Streptomyces antibioticus
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 276090.48

構造登録者

Parisi, G.,Savino, C.,Montemiglio, L.C.,Vallone, B. (登録日: 2016-12-13, 公開日: 2018-02-28, 最終更新日: 2024-01-17)

主引用文献

Parisi, G.,Montemiglio, L.C.,Giuffre, A.,Macone, A.,Scaglione, A.,Cerutti, G.,Exertier, C.,Savino, C.,Vallone, B.
Substrate-induced conformational change in cytochrome P450 OleP.
FASEB J., 33:1787-1800, 2019

PubMed Abstract: The regulation of cytochrome P450 activity is often achieved by structural transitions induced by substrate binding. We describe the conformational transition experienced upon binding by the P450 OleP, an epoxygenase involved in oleandomycin biosynthesis. OleP bound to the substrate analog 6DEB crystallized in 2 forms: one with an ensemble of open and closed conformations in the asymmetric unit and another with only the closed conformation. Characterization of OleP-6DEB binding kinetics, also using the P450 inhibitor clotrimazole, unveiled a complex binding mechanism that involves slow conformational rearrangement with the accumulation of a spectroscopically detectable intermediate where 6DEB is bound to open OleP. Data reported herein provide structural snapshots of key precatalytic steps in the OleP reaction and explain how structural rearrangements induced by substrate binding regulate activity.-Parisi, G., Montemiglio, L. C., Giuffrè, A., Macone, A., Scaglione, A., Cerutti, G., Exertier, C., Savino, C., Vallone, B. Substrate-induced conformational change in cytochrome P450 OleP.

PubMed: 30207799
DOI: 10.1096/fj.201800450RR

実験手法

X-RAY DIFFRACTION (2.62 Å)