1dz9
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Members of the cytochrome P450 superfamily catalyze the addition of, molecular oxygen to nonactivated hydrocarbons at physiological, temperature-a reaction that requires high temperature to proceed in the, absence of a catalyst. Structures were obtained for three intermediates in, the hydroxylation reaction of camphor by P450cam with trapping techniques, and cryocrystallography. The structure of the ferrous dioxygen adduct of, P450cam was determined with 0.91 angstrom wavelength x-rays; irradiation, with 1.5 angstrom x-rays results in breakdown of the dioxygen molecule to, an intermediate that would be consistent with an oxyferryl species. The, structures show conformational changes in several important residues and, reveal a network of bound water molecules that may provide the protons, . | + | Members of the cytochrome P450 superfamily catalyze the addition of, molecular oxygen to nonactivated hydrocarbons at physiological, temperature-a reaction that requires high temperature to proceed in the, absence of a catalyst. Structures were obtained for three intermediates in, the hydroxylation reaction of camphor by P450cam with trapping techniques, and cryocrystallography. The structure of the ferrous dioxygen adduct of, P450cam was determined with 0.91 angstrom wavelength x-rays; irradiation, with 1.5 angstrom x-rays results in breakdown of the dioxygen molecule to, an intermediate that would be consistent with an oxyferryl species. The, structures show conformational changes in several important residues and, reveal a network of bound water molecules that may provide the protons, needed for the reaction. |
==About this Structure== | ==About this Structure== | ||
| - | 1DZ9 is a | + | 1DZ9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with K, HEM, O, CAM and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Sites: K1, K2, K3 and OXO. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DZ9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: reaction intermediate]] | [[Category: reaction intermediate]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:56:35 2007'' |
Revision as of 10:51, 5 November 2007
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PUTATIVE OXO COMPLEX OF P450CAM FROM PSEUDOMONAS PUTIDA
Overview
Members of the cytochrome P450 superfamily catalyze the addition of, molecular oxygen to nonactivated hydrocarbons at physiological, temperature-a reaction that requires high temperature to proceed in the, absence of a catalyst. Structures were obtained for three intermediates in, the hydroxylation reaction of camphor by P450cam with trapping techniques, and cryocrystallography. The structure of the ferrous dioxygen adduct of, P450cam was determined with 0.91 angstrom wavelength x-rays; irradiation, with 1.5 angstrom x-rays results in breakdown of the dioxygen molecule to, an intermediate that would be consistent with an oxyferryl species. The, structures show conformational changes in several important residues and, reveal a network of bound water molecules that may provide the protons, needed for the reaction.
About this Structure
1DZ9 is a Single protein structure of sequence from Pseudomonas putida with K, HEM, O, CAM and TRS as ligands. Structure known Active Sites: K1, K2, K3 and OXO. Full crystallographic information is available from OCA.
Reference
The catalytic pathway of cytochrome p450cam at atomic resolution., Schlichting I, Berendzen J, Chu K, Stock AM, Maves SA, Benson DE, Sweet RM, Ringe D, Petsko GA, Sligar SG, Science. 2000 Mar 3;287(5458):1615-22. PMID:10698731
Page seeded by OCA on Mon Nov 5 12:56:35 2007
Categories: Pseudomonas putida | Single protein | Benson, D.E. | Berendzen, J. | Chu, K. | Maves, S.A. | Petsko, G.A. | Ringe, D. | Schlichting, I. | Sligar, S.G. | Stock, A.M. | Sweet, R.M. | CAM | HEM | K | O | TRS | Heme | Mono-oxygenase | Reaction intermediate
