2c1v

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(New page: 200px<br /> <applet load="2c1v" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c1v, resolution 1.20&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:2c1v.gif|left|200px]]<br />
 
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<applet load="2c1v" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2c1v, resolution 1.20&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE DI-HAEM CYTOCHROME C PEROXIDASE FROM PARACOCCUS PANTOTROPHUS- MIXED VALENCE FORM'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE DI-HAEM CYTOCHROME C PEROXIDASE FROM PARACOCCUS PANTOTROPHUS - Mixed VALENCE FORM==
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Bacterial cytochrome c peroxidases contain an electron transferring (E), heme domain and a peroxidatic (P) heme domain. All but one of these, enzymes are isolated in an inactive oxidized state and require reduction, of the E heme by a small redox donor protein in order to activate the P, heme. Here we present the structures of the inactive oxidized and active, mixed valence enzyme from Paracoccus pantotrophus. Chain flexibility in, the former, as expressed by the crystallographic temperature factors, is, strikingly distributed in certain loop regions, and these coincide with, the regions of conformational change that occur in forming the active, mixed valence enzyme. On the basis of these changes, we postulate a series, of events that occur to link the trigger of the electron entering the ... [[http://ispc.weizmann.ac.il/pmbin/getpm?16407070 (full description)]]
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<StructureSection load='2c1v' size='340' side='right'caption='[[2c1v]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2c1v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_pantotrophus Paracoccus pantotrophus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C1V FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c1v OCA], [https://pdbe.org/2c1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c1v RCSB], [https://www.ebi.ac.uk/pdbsum/2c1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c1v ProSAT]</span></td></tr>
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c1/2c1v_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2c1v ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Bacterial cytochrome c peroxidases contain an electron transferring (E) heme domain and a peroxidatic (P) heme domain. All but one of these enzymes are isolated in an inactive oxidized state and require reduction of the E heme by a small redox donor protein in order to activate the P heme. Here we present the structures of the inactive oxidized and active mixed valence enzyme from Paracoccus pantotrophus. Chain flexibility in the former, as expressed by the crystallographic temperature factors, is strikingly distributed in certain loop regions, and these coincide with the regions of conformational change that occur in forming the active mixed valence enzyme. On the basis of these changes, we postulate a series of events that occur to link the trigger of the electron entering the E heme from either pseudoazurin or cytochrome c(550) and the dissociation of a coordinating histidine at the P heme, which allows substrate access.
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==About this Structure==
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Activation and catalysis of the di-heme cytochrome c peroxidase from Paracoccus pantotrophus.,Echalier A, Goodhew CF, Pettigrew GW, Fulop V Structure. 2006 Jan;14(1):107-17. PMID:16407070<ref>PMID:16407070</ref>
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2C1V is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Paracoccus_pantotrophus Paracoccus pantotrophus]] with CA, HEC and EDO as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C1V OCA]].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Activation and catalysis of the di-heme cytochrome c peroxidase from Paracoccus pantotrophus., Echalier A, Goodhew CF, Pettigrew GW, Fulop V, Structure. 2006 Jan;14(1):107-17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16407070 16407070]
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</div>
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[[Category: Paracoccus pantotrophus]]
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<div class="pdbe-citations 2c1v" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Echalier, A.]]
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[[Category: Fulop, V.]]
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[[Category: CA]]
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[[Category: EDO]]
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[[Category: HEC]]
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[[Category: electron transport]]
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[[Category: heme]]
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[[Category: oxidoreductase]]
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[[Category: periplasmic]]
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[[Category: peroxidase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:41:30 2007''
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==See Also==
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*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Paracoccus pantotrophus]]
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[[Category: Echalier A]]
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[[Category: Fulop V]]

Current revision

CRYSTAL STRUCTURE OF THE DI-HAEM CYTOCHROME C PEROXIDASE FROM PARACOCCUS PANTOTROPHUS - Mixed VALENCE FORM

PDB ID 2c1v

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