3FJO

Structure of chimeric YH CPR

Summary for 3FJO

• Entry DOI: 10.2210/pdb3fjo/pdb
• Related: 1AMO 2BF4
• Descriptor: NADPH-cytochrome P450 reductase, FLAVIN MONONUCLEOTIDE, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: fmn and fad domains of cpr, oxidoreductase, endoplasmic reticulum, flavoprotein, membrane, nadp, phosphoprotein, transmembrane, congenital adrenal hyperplasia, disease mutation
• Biological source: Saccharomyces cerevisiae (Baker's yeast, Human); More
• Cellular location: Endoplasmic reticulum membrane ; Single-pass membrane protein ; Cytoplasmic side : P16435
• Total number of polymer chains: 1
• Total formula weight: 72661.22

Authors

Morera, S.,Aigrain, L.,Truan, G. (deposition date: 2008-12-15, release date: 2009-06-16, Last modification date: 2023-11-01)

Primary citation

Aigrain, L.,Pompon, D.,Morera, S.,Truan, G.
Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase
Embo Rep., 10:742-747, 2009

PubMed Abstract: Two catalytic domains, bearing FMN and FAD cofactors, joined by a connecting domain, compose the core of the NADPH cytochrome P450 reductase (CPR). The FMN domain of CPR mediates electron shuttling from the FAD domain to cytochromes P450. Together, both enzymes form the main mixed-function oxidase system that participates in the metabolism of endo- and xenobiotic compounds in mammals. Available CPR structures show a closed conformation, with the two cofactors in tight proximity, which is consistent with FAD-to-FMN, but not FMN-to-P450, electron transfer. Here, we report the 2.5 A resolution crystal structure of a functionally competent yeast-human chimeric CPR in an open conformation, compatible with FMN-to-P450 electron transfer. Comparison with closed structures shows a major conformational change separating the FMN and FAD cofactors from 86 A.

PubMed: 19483672
DOI: 10.1038/embor.2009.82

Experimental method

X-RAY DIFFRACTION (2.5 Å)