PMID:8342039

Citation	Ravichandran, KG, Boddupalli, SS, Hasermann, CA, Peterson, JA and Deisenhofer, J (1993) Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's. Science 261:731-6
Abstract	Cytochrome P450BM-3, a bacterial fatty acid monoxygenase, resembles the eukaryotic microsomal P450's and their flavoprotein reductase in primary structure and function. The three-dimensional structure of the hemoprotein domain of P450BM-3 was determined by x-ray diffraction and refined to an R factor of 16.9 percent at 2.0 angstrom resolution. The structure consists of an alph and a beta domain. The active site heme is accessible through a long hydrophobic channel formed primarily by the beta domain and the B' and F helices of the alpha domain. The two molecules in the asymmetric unit differ in conformation around the substrate binding pocket. Substantial differences between P450BM-3 and P450cam, the only other P450 structure available, are observed around the substrate binding pocket and the regions important for redox partner binding. A general mechanism for proton transfer in P450's is also proposed.
Links	PubMed
Keywords	Amino Acid Sequence; Bacterial Proteins; Binding Sites; Computer Graphics; Crystallization; Cytochrome P-450 Enzyme System/chemistry; Heme/chemistry; Mixed Function Oxygenases/chemistry; Models, Molecular; Molecular Sequence Data; NADPH-Ferrihemoprotein Reductase; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Alignment; X-Ray Diffraction
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