Publication Date:
1993-08-06
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ravichandran, K G -- Boddupalli, S S -- Hasermann, C A -- Peterson, J A -- Deisenhofer, J -- GM43479/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Aug 6;261(5122):731-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas 75235-9050.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8342039" target="_blank"〉PubMed〈/a〉
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
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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