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PDBsum entry 3cpp

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Oxidoreductase(oxygenase) PDB id
3cpp
Contents
Protein chain
405 a.a.
Ligands
HEM-CMO
CAM
Waters ×238

References listed in PDB file
Key reference
Title Crystal structure of the carbon monoxide-Substrate-Cytochrome p-450cam ternary complex.
Authors R.Raag, T.L.Poulos.
Ref. Biochemistry, 1989, 28, 7586-7592.
PubMed id 2611203
Abstract
The crystal structure of the ternary complex formed between carbon monoxide (CO), camphor, and ferrous cytochrome P-450CAM has been refined to an R value of 17.9% at 1.9-A resolution. To accommodate the CO molecule, the substrate, camphor, moves about 0.8 A while at the same time remaining in nonbonded contact with CO. The average temperature factor of the camphor atoms is about 50% higher in the CO complex, suggesting that the camphor is more loosely bound in this ternary complex. The Fe-C-O angle is about 166 degrees, and thus, CO appears to be bent from the heme normal, as it is in various CO-globin complexes, due to steric interactions with active site groups. The oxygen atom of the CO molecule is nestled into a groove formed by an unusual helical hydrogen bond in the distal helix between the highly conserved Thr 252 and Gly 248 residues. In the transition from the ferric camphor-bound binary complex to the ferrous CO-camphor-bound ternary complex, the heme iron atom moves into the plane defined by the pyrrole nitrogens by about 0.41 A. Although the axial Cys ligand also moves toward the heme, the S-Fe bond stretches from about 2.20 A in the absence of CO to about 2.41 A once CO has bound.
Secondary reference #1
Title The structural basis for substrate-Induced changes in redox potential and spin equilibrium in cytochrome p-450cam.
Authors R.Raag, T.L.Poulos.
Ref. Biochemistry, 1989, 28, 917-922. [DOI no: 10.1021/bi00428a077]
PubMed id 2713354
Full text Abstract
Secondary reference #2
Title High-Resolution crystal structure of cytochrome p450cam.
Authors T.L.Poulos, B.C.Finzel, A.J.Howard.
Ref. J Mol Biol, 1987, 195, 687-700.
PubMed id 3656428
Abstract
Secondary reference #3
Title The 2.6-A crystal structure of pseudomonas putida cytochrome p-450.
Authors T.L.Poulos, B.C.Finzel, I.C.Gunsalus, G.C.Wagner, J.Kraut.
Ref. J Biol Chem, 1985, 260, 16122-16130.
PubMed id 4066706
Abstract
Secondary reference #4
Title Crystal structure of substrate-Free pseudomonas putida cytochrome p-450.
Authors T.L.Poulos, B.C.Finzel, A.J.Howard.
Ref. Biochemistry, 1986, 25, 5314-5322. [DOI no: 10.1021/bi00366a049]
PubMed id 3768350
Full text Abstract
Secondary reference #5
Title Heme enzyme structure and function
Authors T.L.Poulos, B.C.Finzel.
Ref. pept protein rev, 1984, 4, 115.
Secondary reference #6
Title Preliminary crystallographic data on cytochrome p-450cam.
Authors T.L.Poulos, M.Perez, G.C.Wagner.
Ref. J Biol Chem, 1982, 257, 10427-10429.
PubMed id 7107613
Abstract
Secondary reference #7
Title The primary structure of the monoxygenase cytochrome p450cam.
Authors M.Haniu, L.G.Armes, M.Tanaka, K.T.Yasunobu, B.S.Shastry, G.C.Wagner, I.C.Gunsalus.
Ref. Biochem Biophys Res Commun, 1982, 105, 889-894.
PubMed id 7092907
Abstract
PROCHECK
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