1amo
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(New page: 200px<br /><applet load="1amo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1amo, resolution 2.6Å" /> '''THREE-DIMENSIONAL STR...)
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Revision as of 08:50, 20 November 2007
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THREE-DIMENSIONAL STRUCTURE OF NADPH-CYTOCHROME P450 REDUCTASE: PROTOTYPE FOR FMN-AND FAD-CONTAINING ENZYMES
Overview
Microsomal NADPH-cytochrome P450 reductase (CPR) is one of only two, mammalian enzymes known to contain both FAD and FMN, the other being, nitric-oxide synthase. CPR is a membrane-bound protein and catalyzes, electron transfer from NADPH to all known microsomal cytochromes P450. The, structure of rat liver CPR, expressed in Escherichia coli and solubilized, by limited trypsinolysis, has been determined by x-ray crystallography at, 2.6 A resolution. The molecule is composed of four structural domains:, (from the N- to C- termini) the FMN-binding domain, the connecting domain, and the FAD- and NADPH-binding domains. The FMN-binding domain is similar, to the structure of flavodoxin, whereas the two C-terminal, dinucleotide-binding domains are similar to those of ferredoxin-NADP+, reductase (FNR). The connecting domain, situated between the FMN-binding, and FNR-like domains, is responsible for the relative orientation of the, other domains, ensuring the proper alignment of the two flavins necessary, for efficient electron transfer. The two flavin isoalloxazine rings are, juxtaposed, with the closest distance between them being about 4 A. The, bowl-shaped surface near the FMN-binding site is likely the docking site, of cytochrome c and the physiological redox partners, including, cytochromes P450 and b5 and heme oxygenase.
About this Structure
1AMO is a Single protein structure of sequence from Rattus norvegicus with FAD, FMN and NAP as ligands. Active as NADPH--hemoprotein reductase, with EC number 1.6.2.4 Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes., Wang M, Roberts DL, Paschke R, Shea TM, Masters BS, Kim JJ, Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8411-6. PMID:9237990
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