1cpt
From Proteopedia
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| - | [[Image:1cpt.jpg|left|200px]] | + | [[Image:1cpt.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE AND REFINEMENT OF CYTOCHROME P450-TERP AT 2.3 ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 1cpt |SIZE=350|CAPTION= <scene name='initialview01'>1cpt</scene>, resolution 2.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE AND REFINEMENT OF CYTOCHROME P450-TERP AT 2.3 ANGSTROMS RESOLUTION''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CPT is a [ | + | 1CPT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CPT OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8120894 8120894] |
[[Category: Pseudomonas sp.]] | [[Category: Pseudomonas sp.]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxidoreductase(oxygenase)]] | [[Category: oxidoreductase(oxygenase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:27:22 2008'' |
Revision as of 08:27, 20 March 2008
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| , resolution 2.3Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.. 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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