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[[Image:2c1v.gif|left|200px]]
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{{STRUCTURE_2c1v|  PDB=2c1v  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF THE DI-HAEM CYTOCHROME C PEROXIDASE FROM PARACOCCUS PANTOTROPHUS- MIXED VALENCE FORM'''


==CRYSTAL STRUCTURE OF THE DI-HAEM CYTOCHROME C PEROXIDASE FROM PARACOCCUS PANTOTROPHUS - Mixed VALENCE FORM==
<StructureSection load='2c1v' size='340' side='right'caption='[[2c1v]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== 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/c1/2c1v_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2c1v ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2C1V is a [[Single protein]] structure of sequence from [http://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].
</div>
<div class="pdbe-citations 2c1v" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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://www.ncbi.nlm.nih.gov/pubmed/16407070 16407070]
*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
[[Category: Cytochrome-c peroxidase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Paracoccus pantotrophus]]
[[Category: Paracoccus pantotrophus]]
[[Category: Single protein]]
[[Category: Echalier A]]
[[Category: Echalier, A.]]
[[Category: Fulop V]]
[[Category: Fulop, V.]]
[[Category: Electron transport]]
[[Category: Heme]]
[[Category: Oxidoreductase,periplasmic]]
[[Category: Peroxidase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 21:07:08 2008''

Latest revision as of 05:08, 17 October 2024

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

2c1v, resolution 1.20Å

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