1CPT

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

Summary for 1CPT

• Entry DOI: 10.2210/pdb1cpt/pdb
• Descriptor: CYTOCHROME P450-TERP, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: oxidoreductase(oxygenase)
• Biological source: Pseudomonas sp.
• Cellular location: Cytoplasm (By similarity): P33006
• Total number of polymer chains: 1
• Total formula weight: 48593.69

Authors

Hasemann, C.A.,Ravichandran, K.G.,Peterson, J.A.,Deisenhofer, J. (deposition date: 1993-11-23, release date: 1994-01-31, Last modification date: 2024-02-07)

Primary citation

Hasemann, C.A.,Ravichandran, K.G.,Peterson, J.A.,Deisenhofer, J.
Crystal structure and refinement of cytochrome P450terp at 2.3 A resolution.
J.Mol.Biol., 236:1169-1185, 1994

PubMed Abstract: 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.

PubMed: 8120894
DOI: 10.1016/0022-2836(94)90019-1

Experimental method

X-RAY DIFFRACTION (2.3 Å)