3BUJ

Crystal Structure of CalO2

3BUJ の概要

• エントリーDOI: 10.2210/pdb3buj/pdb
• 分子名称: CalO2, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: p450, heme, iron, metal-binding, monooxygenase, oxidoreductase, metal binding protein
• 由来する生物種: Micromonospora echinospora
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44587.52

構造登録者

McCoy, J.G.,Johnson, H.D.,Singh, S.,Bingman, C.A.,Thorson, J.S.,Phillips Jr., G.N. (登録日: 2008-01-02, 公開日: 2008-04-29, 最終更新日: 2023-08-30)

主引用文献

McCoy, J.G.,Johnson, H.D.,Singh, S.,Bingman, C.A.,Lei, I.K.,Thorson, J.S.,Phillips Jr., G.N.
Structural characterization of CalO2: a putative orsellinic acid P450 oxidase in the calicheamicin biosynthetic pathway.
Proteins, 74:50-60, 2009

PubMed Abstract: Although bacterial iterative Type I polyketide synthases are now known to participate in the biosynthesis of a small set of diverse natural products, the subsequent downstream modification of the resulting polyketide products remains poorly understood. Toward this goal, we report the X-ray structure determination at 2.5 A resolution and preliminary characterization of the putative orsellenic acid P450 oxidase (CalO2) involved in calicheamicin biosynthesis. These studies represent the first crystal structure for a P450 involved in modifying a bacterial iterative Type I polyketide product and suggest the CalO2-catalyzed step may occur after CalO3-catalyzed iodination and may also require a coenzyme A- (CoA) or acyl carrier protein- (ACP) bound substrate. Docking studies also reveal a putative docking site within CalO2 for the CLM orsellinic acid synthase (CalO5) ACP domain which involves a well-ordered helix along the CalO2 active site cavity that is unique compared with other P450 structures.

PubMed: 18561189
DOI: 10.1002/prot.22131

実験手法

X-RAY DIFFRACTION (2.47 Å)