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[[Image:1yrc.gif|left|200px]]


{{Structure
==X-ray Crystal Structure of hydrogenated Cytochrome P450cam==
|PDB= 1yrc |SIZE=350|CAPTION= <scene name='initialview01'>1yrc</scene>, resolution 1.4&Aring;
<StructureSection load='1yrc' size='340' side='right'caption='[[1yrc]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|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>
<table><tr><td colspan='2'>[[1yrc]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YRC FirstGlance]. <br>
|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]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yrc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yrc OCA], [https://pdbe.org/1yrc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yrc RCSB], [https://www.ebi.ac.uk/pdbsum/1yrc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yrc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CPXA_PSEPU CPXA_PSEPU] Involved in a camphor oxidation system.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yr/1yrc_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1yrc ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 (&gt;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.


'''X-ray Crystal Structure of hydrogenated Cytochrome P450cam'''
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<ref>PMID:15858263</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1yrc" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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 (&gt;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.
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
 
== References ==
==About this Structure==
<references/>
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].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
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: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
[[Category: Single protein]]
[[Category: Dauvergne M-T]]
[[Category: Dauvergne, M T.]]
[[Category: Meilleur F]]
[[Category: Meilleur, F.]]
[[Category: Myles DAA]]
[[Category: Myles, D A.A.]]
[[Category: Schlichting I]]
[[Category: Schlichting, I.]]
[[Category: CAM]]
[[Category: HEM]]
[[Category: K]]
[[Category: ferric]]
[[Category: heme]]
[[Category: mono-oxygenase]]
[[Category: oxidoreductase]]
 
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