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5Y1I

The crystal structure of GfsF

Summary for 5Y1I
Entry DOI10.2210/pdb5y1i/pdb
DescriptorCytochrome P450, PROTOPORPHYRIN IX CONTAINING FE, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
Functional Keywordsmonooxygenase, heme, oxidoreductase
Biological sourceStreptomyces graminofaciens
Total number of polymer chains2
Total formula weight90496.74
Authors
Miyanaga, A.,Kudo, F.,Eguchi, T. (deposition date: 2017-07-20, release date: 2017-09-13, Last modification date: 2023-11-22)
Primary citationMiyanaga, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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