1cpt
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(New page: 200px<br /><applet load="1cpt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cpt, resolution 2.3Å" /> '''CRYSTAL STRUCTURE AND...)
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Revision as of 10:32, 20 November 2007
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CRYSTAL STRUCTURE AND REFINEMENT OF CYTOCHROME P450-TERP AT 2.3 ANGSTROMS RESOLUTION
Overview
Cytochrome P450terp is a class I (mitochondrial/bacterial) P450 that, catalyzes the hydroxylation of alpha-terpineol as part of the catabolic, assimilation of this compound by a pseudomonad species. Crystals grown, from the purified protein have the symmetry of space group P6(1)22, and, cell dimensions a = b = 69.4 A, c = 456.6 A, alpha = beta = 90 degrees, gamma = 120 degrees. Diffraction data were collected at the Cornell High, Energy Synchrotron Source, and the structure of P450terp was solved by a, combination of molecular replacement and multiple isomorphous replacement, techniques. A model of P450terp was built and refined against native data, to an R-factor of 18.9% for data with I > or = sigma(I) between 6.0 A and, 2.3 A resolution. This model contains 412 of the 428 P450terp amino acid, residues; the loop between helices F and G is disordered in the crystal., While the overall fold of P450terp is very similar to that of P450cam, only three-quarters of the C alpha positions can be superimposed, to a, root-mean-square deviation of only 1.87 A. The mode of substrate binding, by P450terp can be predicted, and probable substrate contact residues, identified. The heme environment and side-chain positions in the adjacent, I-helix suggest possible modes of proton delivery in the catalytic cycle, of the enzyme.
About this Structure
1CPT is a Single protein structure of sequence from Pseudomonas sp. with HEM as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure and refinement of cytochrome P450terp at 2.3 A resolution., Hasemann CA, Ravichandran KG, Peterson JA, Deisenhofer J, J Mol Biol. 1994 Mar 4;236(4):1169-85. PMID:8120894
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