1dz8: Difference between revisions

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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, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?10698731 (full description)]]
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==
1DZ8 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, OXY, CAM and TRS as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Sites: K1, K2, K3 and O2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DZ8 OCA]].  
1DZ8 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, OXY, CAM and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Sites: K1, K2, K3 and O2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DZ8 OCA].  


==Reference==
==Reference==
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[[Category: mono-oxygenase]]
[[Category: mono-oxygenase]]


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Revision as of 13:51, 5 November 2007

File:1dz8.gif


1dz8, resolution 1.9Å

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OXYGEN COMPLEX OF P450CAM FROM PSEUDOMONAS PUTIDA

OverviewOverview

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 StructureAbout this Structure

1DZ8 is a Single protein structure of sequence from Pseudomonas putida with K, HEM, OXY, CAM and TRS as ligands. Structure known Active Sites: K1, K2, K3 and O2. Full crystallographic information is available from OCA.

ReferenceReference

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

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