Molecular modeling of the 3-D structure of cytochrome P-450scc.
Sequence-alignment studies of the bovine mitochondrial cholesterol side-chain cleavage enzyme cytochrome P-450scc with the bacterial cytochrome P-450cam (camphor hydroxylating enzyme) have been undertaken. Our novel alignment of the sequences revealed 69 identical residues and many highly conserved regions. The results of the sequence alignment studies were used to model the 3-D structure of P-450scc based on the available crystal structure of P-450cam. The major insertions in the sequence are found mainly on four external-loop regions of the molecule, while the core structure of P-450cam is retained with subtle internal modifications. The most hydrophobic of these four external loops is proposed as a candidate for membrane attachment.
Vijayakumar
S
S
Department of Biology, Rensselaer Polytechnic Institute, Troy, NY 12180-3590.
Salerno
J C
JC
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002164:Camphor / Q000378:metabolism; D002417:Cattle; D002784:Cholesterol / Q000378:metabolism; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D002164:Camphor; D003577:Cytochrome P-450 Enzyme System; D002784:Cholesterol