Crystallization and preliminary x-ray studies of NADPH-cytochrome P450 reductase. Proc Natl Acad Sci U S A 1995 Apr 11;92(8):3214-8
Date
04/11/1995Pubmed ID
7724541Pubmed Central ID
PMC42136DOI
10.1073/pnas.92.8.3214Scopus ID
2-s2.0-0028985593 (requires institutional sign-in at Scopus site) 29 CitationsAbstract
NADPH-cytochrome P450 reductase (CPR; NADPH:ferrihemoprotein reductase, EC 1.6.2.4) catalyzes the transfer of electrons to all known microsomal cytochromes P450. CPR is unique in that it is one of only two mammalian enzymes known to contain both flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN), the other being the various isoforms of nitric oxide synthase. Similarities in amino acid sequence and in functional domain arrangement with other key flavoproteins, including nitric oxide synthase, make CPR an excellent prototype for studies of interactions between two flavin cofactors. We have obtained diffraction-quality crystals of rat liver CPR, expressed in Escherichia coli and solubilized by limited proteolysis with trypsin. The crystals were grown in Hepes buffer (pH 7.0), containing polyethylene glycol 4500 and NaCl. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions a = 103.3 A, b = 116.1 A, and c = 120.4 A. If we assume that there are two molecules of the 72-kDa CPR polypeptide per asymmetric unit, the calculated value of Vm is 2.54 A3/Da.
Author List
Djordjevic S, Roberts DL, Wang M, Shea T, Camitta MG, Masters BS, Kim JJAuthor
Bruce m. Camitta Professor in the Pediatrics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceAnimals
Crystallization
Crystallography, X-Ray
Escherichia coli
Liver
Molecular Sequence Data
NADPH-Ferrihemoprotein Reductase
Rats
Recombinant Proteins
