1yrd
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1yrd |SIZE=350|CAPTION= <scene name='initialview01'>1yrd</scene>, resolution 1.7Å | |PDB= 1yrd |SIZE=350|CAPTION= <scene name='initialview01'>1yrd</scene>, resolution 1.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= cyp101 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 Pseudomonas putida]) | |GENE= cyp101 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 Pseudomonas putida]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1yrc|1YRC]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yrd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yrd OCA], [http://www.ebi.ac.uk/pdbsum/1yrd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yrd RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Myles, D A.A.]] | [[Category: Myles, D A.A.]] | ||
[[Category: Schlichting, I.]] | [[Category: Schlichting, I.]] | ||
| - | [[Category: CAM]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: K]] | ||
[[Category: ferric]] | [[Category: ferric]] | ||
[[Category: heme]] | [[Category: heme]] | ||
| Line 36: | Line 36: | ||
[[Category: perdeuterated protein]] | [[Category: perdeuterated protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:19:09 2008'' |
Revision as of 22:19, 30 March 2008
| |||||||
| , resolution 1.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | cyp101 (Pseudomonas putida) | ||||||
| Activity: | Camphor 5-monooxygenase, with EC number 1.14.15.1 | ||||||
| Related: | 1YRC
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-ray crystal structure of PERDEUTERATED Cytochrome P450cam
Overview
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 Structure
1YRD is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.
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:15858263
Page seeded by OCA on Mon Mar 31 01:19:09 2008
