1cpt
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1cpt |SIZE=350|CAPTION= <scene name='initialview01'>1cpt</scene>, resolution 2.3Å | |PDB= 1cpt |SIZE=350|CAPTION= <scene name='initialview01'>1cpt</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cpt OCA], [http://www.ebi.ac.uk/pdbsum/1cpt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cpt RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Peterson, J A.]] | [[Category: Peterson, J A.]] | ||
[[Category: Ravichandran, K G.]] | [[Category: Ravichandran, K G.]] | ||
| - | [[Category: HEM]] | ||
[[Category: oxidoreductase(oxygenase)]] | [[Category: oxidoreductase(oxygenase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:26:18 2008'' |
Revision as of 16:26, 30 March 2008
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Sun Mar 30 19:26:18 2008
