1cpt: Difference between revisions

Revision as of 21:04, 30 June 2008

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File:1cpt.png

Template:STRUCTURE 1cpt

CRYSTAL STRUCTURE AND REFINEMENT OF CYTOCHROME P450-TERP AT 2.3 ANGSTROMS RESOLUTIONCRYSTAL STRUCTURE AND REFINEMENT OF CYTOCHROME P450-TERP AT 2.3 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 8120894

About this StructureAbout this Structure

1CPT is a Single protein structure of sequence from Pseudomonas sp.. Full crystallographic information is available from OCA.

ReferenceReference

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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-'''CRYSTAL STRUCTURE AND REFINEMENT OF CYTOCHROME P450-TERP AT 2.3 ANGSTROMS RESOLUTION'''
+===CRYSTAL STRUCTURE AND REFINEMENT OF CYTOCHROME P450-TERP AT 2.3 ANGSTROMS RESOLUTION===
-==Overview==
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-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 &gt; 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.
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+{{ABSTRACT_PUBMED_8120894}}
 ==About this Structure==
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 [[Category: Peterson, J A.]]
 [[Category: Ravichandran, K G.]]
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