Cloning, purification, crystallization and preliminary X-ray analysis of a chimeric NADPH-cytochrome P450 reductase.
NADPH-cytochrome P450 reductase (CPR) is the favoured redox partner of microsomal cytochromes P450. This protein is composed of two flavin-containing domains (FMN and FAD) connected by a structured linker. An active CPR chimera consisting of the yeast FMN and human FAD domains has been produced, purified and crystallized. The crystals belonged to the monoclinic space group C2 and contained one molecule per asymmetric unit. Molecular replacement was performed using the published rat and yeast structures as search models. The initial electron-density maps revealed that the chimeric enzyme had crystallized in a conformation that differed from those of previously solved structures.
Aigrain
Louise
L
Laboratoire d'Ingénierie des Protéines Membranaires, CNRS, Gif-sur-Yvette, France.
Pompon
Denis
D
Truan
Gilles
G
Moréra
Solange
S
D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D009251:NADPH-Ferrihemoprotein Reductase / Q000737:chemistry* / Q000302:isolation & purification*; D011993:Recombinant Fusion Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D012441:Saccharomyces cerevisiae
D011993:Recombinant Fusion Proteins; D009251:NADPH-Ferrihemoprotein Reductase