2HPD

CRYSTAL STRUCTURE OF HEMOPROTEIN DOMAIN OF P450BM-3, A PROTOTYPE FOR MICROSOMAL P450'S

Summary for 2HPD

• Entry DOI: 10.2210/pdb2hpd/pdb
• Descriptor: CYTOCHROME P450 BM-3, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: oxidoreductase(oxygenase)
• Biological source: Bacillus megaterium
• Cellular location: Cytoplasm (By similarity): P14779
• Total number of polymer chains: 2
• Total formula weight: 108825.56

Authors

Ravichandran, K.G.,Boddupalli, S.S.,Hasemann, C.A.,Peterson, J.A.,Deisenhofer, J. (deposition date: 1993-09-16, release date: 1993-10-31, Last modification date: 2024-02-14)

Primary citation

Ravichandran, K.G.,Boddupalli, S.S.,Hasermann, C.A.,Peterson, J.A.,Deisenhofer, J.
Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's.
Science, 261:731-736, 1993

PubMed 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.

PubMed: 8342039

Experimental method

X-RAY DIFFRACTION (2 Å)