1yrc: Difference between revisions
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[[Image:1yrc.gif|left|200px]] | [[Image:1yrc.gif|left|200px]] | ||
'''X-ray Crystal Structure of hydrogenated Cytochrome P450cam''' | {{Structure | ||
|PDB= 1yrc |SIZE=350|CAPTION= <scene name='initialview01'>1yrc</scene>, resolution 1.4Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=CAM:CAMPHOR'>CAM</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] | |||
|GENE= | |||
}} | |||
'''X-ray Crystal Structure of hydrogenated Cytochrome P450cam''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1YRC is a [ | 1YRC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YRC OCA]. | ||
==Reference== | ==Reference== | ||
Production and X-ray crystallographic analysis of fully deuterated cytochrome P450cam., Meilleur F, Dauvergne MT, Schlichting I, Myles DA, Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):539-44. Epub 2005, Apr 20. PMID:[http:// | Production and X-ray crystallographic analysis of fully deuterated cytochrome P450cam., Meilleur F, Dauvergne MT, Schlichting I, Myles DA, Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):539-44. Epub 2005, Apr 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15858263 15858263] | ||
[[Category: Camphor 5-monooxygenase]] | [[Category: Camphor 5-monooxygenase]] | ||
[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:26:29 2008'' | ||
Revision as of 16:26, 20 March 2008
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| , resolution 1.4Å | |||||||
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| Ligands: | , and | ||||||
| Activity: | Camphor 5-monooxygenase, with EC number 1.14.15.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-ray Crystal Structure of hydrogenated Cytochrome P450cam
OverviewOverview
Neutron protein crystallography allows H-atom positions to be located in biological structures at the relatively modest resolution of 1.5-2.0 A. A difficulty of this technique arises from the incoherent scattering from hydrogen, which considerably reduces the signal-to-noise ratio of the data. This can be overcome by preparing fully deuterated samples. Efficient protocols for routine and low-cost production of in vivo deuterium-enriched proteins have been developed. Here, the overexpression and crystallization of highly (>99%) deuterium-enriched cytochrome P450cam for neutron analysis is reported. Cytochrome P450cam from Pseudomonas putida catalyses the hydroxylation of camphor from haem-bound molecular O(2) via a mechanism that is thought to involve a proton-shuttle pathway to the active site. Since H atoms cannot be visualized in available X-ray structures, neutron diffraction is being used to determine the protonation states and water structure at the active site of the enzyme. Analysis of both hydrogenated and perdeuterated P450cam showed no significant changes between the X-ray structures determined at 1.4 and 1.7 A, respectively. This work demonstrates that the fully deuterated protein is highly isomorphous with the native (hydrogenated) protein and is appropriate for neutron protein crystallographic analysis.
About this StructureAbout this Structure
1YRC is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.
ReferenceReference
Production and X-ray crystallographic analysis of fully deuterated cytochrome P450cam., Meilleur F, Dauvergne MT, Schlichting I, Myles DA, Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):539-44. Epub 2005, Apr 20. PMID:15858263
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