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[[Image:1kok.gif|left|200px]]
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{{STRUCTURE_1kok|  PDB=1kok  |  SCENE=  }}
'''Crystal Structure of Mesopone Cytochrome c Peroxidase (MpCcP)'''


==Crystal Structure of Mesopone Cytochrome c Peroxidase (MpCcP)==
<StructureSection load='1kok' size='340' side='right'caption='[[1kok]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1kok]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KOK 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]] 1.7&#8491;</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=1kok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kok OCA], [https://pdbe.org/1kok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kok RCSB], [https://www.ebi.ac.uk/pdbsum/1kok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kok ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CCPR_YEAST CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
== 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/ko/1kok_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=1kok ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The effect of heme ring oxygenation on enzyme structure and function has been examined in a reconstituted cytochrome c peroxidase. Oxochlorin derivatives were formed by OsO(4) treatment of mesoporphyrin followed by acid-catalyzed pinacol rearrangement. The northern oxochlorin isomers were isolated by chromatography, and the regio-isomers assignments determined by 2D COSY and NOE 1H NMR. The major isomer, 4-mesoporphyrinone (Mp), was metallated with FeCl(2) and reconstituted into cytochrome c peroxidase (CcP) forming a hybrid green protein, MpCcP. The heme-altered enzyme has 99% wild-type peroxidase activity with cytochrome c. EPR spectroscopy of MpCcP intermediate compound I verifies the formation of the Trp(191) radical similar to wild-type CcP in the reaction cycle. Peroxidase activity with small molecules is varied: guaiacol turnover increases approximately five-fold while that with ferrocyanide is approximately 85% of native. The electron-withdrawing oxo-substitutents on the cofactor cause a approximately 60-mV increase in Fe(III)/Fe(II) reduction potential. The present investigation represents the first structural characterization of an oxochlorin protein with X-ray intensity data collected to 1.70 A. Although a mixture of R- and S-mesopone isomers of the FeMP cofactor was used during heme incorporation into the apo-protein, only the S-isomer is found in the crystallized protein.


==Overview==
Mesopone cytochrome c peroxidase: functional model of heme oxygenated oxidases.,Immoos CE, Bhaskar B, Cohen MS, Barrows TP, Farmer PJ, Poulos TL J Inorg Biochem. 2002 Sep 20;91(4):635-43. PMID:12237229<ref>PMID:12237229</ref>
The effect of heme ring oxygenation on enzyme structure and function has been examined in a reconstituted cytochrome c peroxidase. Oxochlorin derivatives were formed by OsO(4) treatment of mesoporphyrin followed by acid-catalyzed pinacol rearrangement. The northern oxochlorin isomers were isolated by chromatography, and the regio-isomers assignments determined by 2D COSY and NOE 1H NMR. The major isomer, 4-mesoporphyrinone (Mp), was metallated with FeCl(2) and reconstituted into cytochrome c peroxidase (CcP) forming a hybrid green protein, MpCcP. The heme-altered enzyme has 99% wild-type peroxidase activity with cytochrome c. EPR spectroscopy of MpCcP intermediate compound I verifies the formation of the Trp(191) radical similar to wild-type CcP in the reaction cycle. Peroxidase activity with small molecules is varied: guaiacol turnover increases approximately five-fold while that with ferrocyanide is approximately 85% of native. The electron-withdrawing oxo-substitutents on the cofactor cause a approximately 60-mV increase in Fe(III)/Fe(II) reduction potential. The present investigation represents the first structural characterization of an oxochlorin protein with X-ray intensity data collected to 1.70 A. Although a mixture of R- and S-mesopone isomers of the FeMP cofactor was used during heme incorporation into the apo-protein, only the S-isomer is found in the crystallized protein.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1KOK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOK OCA].
</div>
<div class="pdbe-citations 1kok" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Mesopone cytochrome c peroxidase: functional model of heme oxygenated oxidases., Immoos CE, Bhaskar B, Cohen MS, Barrows TP, Farmer PJ, Poulos TL, J Inorg Biochem. 2002 Sep 20;91(4):635-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12237229 12237229]
*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
[[Category: Cytochrome-c peroxidase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Barrows TP]]
[[Category: Barrows, T P.]]
[[Category: Bhaskar B]]
[[Category: Bhaskar, B.]]
[[Category: Cohen MS]]
[[Category: Cohen, M S.]]
[[Category: Farmer PJ]]
[[Category: Farmer, P J.]]
[[Category: Immoos CE]]
[[Category: Immoos, C E.]]
[[Category: Poulos TL]]
[[Category: Poulos, T L.]]
[[Category: Bifunctional catalyst]]
[[Category: Cytochrome c peroxidase]]
[[Category: Cytochrome oxidase]]
[[Category: Mesoporphyrin]]
[[Category: Nitrite reducatse]]
[[Category: Proximal loop]]
[[Category: Trp191 cationic radical]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:59:15 2008''

Latest revision as of 06:24, 13 August 2026

Crystal Structure of Mesopone Cytochrome c Peroxidase (MpCcP)

1kok, resolution 1.70Å

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