| | |  | | | | Record from Web of Science® | | | | | | |
| CRYSTAL-STRUCTURE OF HEMOPROTEIN DOMAIN OF P450BM-3, A PROTOTYPE FOR MICROSOMAL P450S |
|
|
| Author(s): RAVICHANDRAN KG, BODDUPALLI SS, HASEMANN CA, PETERSON JA, DEISENHOFER J |
| Source: SCIENCE Volume: 261 Issue: 5122 Pages: 731-736 Published: AUG 6 1993 |
| Times Cited: 736 References: 39 |
| Abstract: Cytochrome P450BM-3, a bacterial fatty acid monooxygenase, 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 alpha 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. |
| Document Type: Article |
| Language: English |
Addresses:
1. UNIV TEXAS, SW MED CTR, HOWARD HUGHES MED INST, 5323 HARRY HINES BLVD, DALLAS, TX 75235 USA
2. UNIV TEXAS, SW MED CTR, DEPT BIOCHEM, DALLAS, TX 75235 USA |
| Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: LQ730 |
| ISSN: 0036-8075 |
|
| | | | | | | | | Record from Web of Science® | | | | | | | | | |