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'''CRYSTAL STRUCTURE OF HEMOPROTEIN DOMAIN OF P450BM-3, A PROTOTYPE FOR MICROSOMAL P450'S''' | '''CRYSTAL STRUCTURE OF HEMOPROTEIN DOMAIN OF P450BM-3, A PROTOTYPE FOR MICROSOMAL P450'S''' | ||
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[[Category: Peterson, J A.]] | [[Category: Peterson, J A.]] | ||
[[Category: Ravichandran, K G.]] | [[Category: Ravichandran, K G.]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:32:48 2008'' | |||
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Revision as of 03:32, 4 May 2008
CRYSTAL STRUCTURE OF HEMOPROTEIN DOMAIN OF P450BM-3, A PROTOTYPE FOR MICROSOMAL P450'S
Overview
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.
About this Structure
2HPD is a Single protein structure of sequence from Bacillus megaterium. Full crystallographic information is available from OCA.
Reference
Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's., Ravichandran KG, Boddupalli SS, Hasermann CA, Peterson JA, Deisenhofer J, Science. 1993 Aug 6;261(5122):731-6. PMID:8342039 Page seeded by OCA on Sun May 4 06:32:48 2008
