Secondary structure prediction of 52 membrane-bound cytochromes P450 shows a strong structural similarity to P450cam.
The secondary structure of 52 aligned cytochrome P450 sequences, all of which are membrane bound, is predicted and collectively compared with the crystal structure of the soluble cytochrome P450cam. Ten of 13 helical regions, 6 of 7 beta-pair regions, and beta-structure corresponding to a known beta-bulge near the active site of P450cam are predicted to exist in the membrane-bound P450s. Three turns associated with beta-structure in the soluble enzyme are also predicted for the membrane-bound forms. A strong structural similarity is evident between membrane P450s and the soluble P450cam. Consequently, a multitransmembrane structure involving much of P450 seems highly unlikely. A structure with two N-terminal transmembrane segments is compatible with these observations.
Nelson
D R
DR
Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston 77225.
Strobel
H W
HW
D000818:Animals; D019475:Camphor 5-Monooxygenase; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D006801:Humans; D008566:Membranes / Q000378:metabolism*; D008928:Mitochondria / Q000378:metabolism; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D011487:Protein Conformation
D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D019475:Camphor 5-Monooxygenase