3fjo

Structure of chimeric YH CPR

spinqualitylabelsall models 3fjo, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3fjo is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FAD, FMN Related: 1amo, 2bf4 Gene: NCP1, POR (HUMAN) Activity: NADPH--hemoprotein reductase, with EC number 1.6.2.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NCPR_YEAST] This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis. Has NADPH-dependent ferrireductase activity on the plasma membrane. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase.,Aigrain L, Pompon D, Morera S, Truan G EMBO Rep. 2009 Jul;10(7):742-7. Epub 2009 May 29. PMID:19483672 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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