5Y1I

The crystal structure of GfsF

5Y1I の概要

• エントリーDOI: 10.2210/pdb5y1i/pdb
• 分子名称: Cytochrome P450, PROTOPORPHYRIN IX CONTAINING FE, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• 機能のキーワード: monooxygenase, heme, oxidoreductase
• 由来する生物種: Streptomyces graminofaciens
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 90496.74

構造登録者

Miyanaga, A.,Kudo, F.,Eguchi, T. (登録日: 2017-07-20, 公開日: 2017-09-13, 最終更新日: 2023-11-22)

主引用文献

Miyanaga, A.,Takayanagi, R.,Furuya, T.,Kawamata, A.,Itagaki, T.,Iwabuchi, Y.,Kanoh, N.,Kudo, F.,Eguchi, T.
Substrate Recognition by a Dual-Function P450 Monooxygenase GfsF Involved in FD-891 Biosynthesis
Chembiochem, 18:2179-2187, 2017

PubMed Abstract: GfsF is a multifunctional P450 monooxygenase that catalyzes epoxidation and subsequent hydroxylation in the biosynthesis of macrolide polyketide FD-891. Here, we describe the biochemical and structural analysis of GfsF. To obtain the structural basis of a dual-function reaction, we determined the crystal structure of ligand-free GfsF, which revealed GfsF to have a predominantly hydrophobic substrate binding pocket. The docking models, in conjunction with the results of the enzymatic assay with substrate analogues and site-directed mutagenesis suggested two distinct substrate binding modes for epoxidation and hydroxylation reactions, which explained how GfsF regulates the order of two oxidative reactions. These findings provide new insights into the reaction mechanism of multifunctional P450 monooxygenases.

PubMed: 28869713
DOI: 10.1002/cbic.201700429

実験手法

X-RAY DIFFRACTION (2 Å)