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| <StructureSection load='1kok' size='340' side='right'caption='[[1kok]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='1kok' size='340' side='right'caption='[[1kok]], [[Resolution|resolution]] 1.70Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1kok]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1KOK FirstGlance]. <br> | | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HIF:FE(III)-(4-MESOPORPHYRINONE)'>HIF</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2cyp|2cyp]]</div></td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HIF:FE(III)-(4-MESOPORPHYRINONE)'>HIF</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OPBYC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] </span></td></tr>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1kok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kok OCA], [http://pdbe.org/1kok PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kok RCSB], [http://www.ebi.ac.uk/pdbsum/1kok PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kok ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/CCPR_YEAST CCPR_YEAST]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | | [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 == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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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=1kok ConSurf]. | | </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="clear:both"></div> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| 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.
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| 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>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 1kok" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]] | | *[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Atcc 18824]]
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| [[Category: Cytochrome-c peroxidase]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Barrows, T P]] | | [[Category: Saccharomyces cerevisiae]] |
| [[Category: Bhaskar, B]] | | [[Category: Barrows TP]] |
| [[Category: Cohen, M S]] | | [[Category: Bhaskar B]] |
| [[Category: Farmer, P J]] | | [[Category: Cohen MS]] |
| [[Category: Immoos, C E]] | | [[Category: Farmer PJ]] |
| [[Category: Poulos, T L]] | | [[Category: Immoos CE]] |
| [[Category: Bifunctional catalyst]]
| | [[Category: Poulos TL]] |
| [[Category: Cytochrome c peroxidase]]
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| [[Category: Cytochrome oxidase]]
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| [[Category: Mesoporphyrin]]
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| [[Category: Nitrite reducatse]]
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| [[Category: Oxidoreductase]]
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| [[Category: Proximal loop]]
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| [[Category: Trp191 cationic radical]]
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