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| | <StructureSection load='4cvj' size='340' side='right'caption='[[4cvj]], [[Resolution|resolution]] 2.18Å' scene=''> | | <StructureSection load='4cvj' size='340' side='right'caption='[[4cvj]], [[Resolution|resolution]] 2.18Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cvj]] 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=4CVJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4CVJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cvj]] 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=4CVJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CVJ FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cvi|4cvi]]</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=4cvj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cvj OCA], [https://pdbe.org/4cvj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cvj RCSB], [https://www.ebi.ac.uk/pdbsum/4cvj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cvj 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>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=4cvj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cvj OCA], [http://pdbe.org/4cvj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cvj RCSB], [http://www.ebi.ac.uk/pdbsum/4cvj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cvj 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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| - | [[Category: Cytochrome-c peroxidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Blakeley, M P]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Casadei, C M]] | + | [[Category: Blakeley MP]] |
| - | [[Category: Gumiero, A]] | + | [[Category: Casadei CM]] |
| - | [[Category: Moody, P C.E]] | + | [[Category: Gumiero A]] |
| - | [[Category: Ostermann, A]] | + | [[Category: Moody PCE]] |
| - | [[Category: Raven, E L]] | + | [[Category: Ostermann A]] |
| - | [[Category: Electron transport]]
| + | [[Category: Raven EL]] |
| - | [[Category: Enzyme intermediate]]
| + | |
| - | [[Category: Ferric]]
| + | |
| - | [[Category: Heme]]
| + | |
| - | [[Category: Heme peroxidase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Protonation]]
| + | |
| - | [[Category: Redox]]
| + | |
| Structural highlights
Function
[CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Publication Abstract from PubMed
Heme enzymes activate oxygen through formation of transient iron-oxo (ferryl) intermediates of the heme iron. A long-standing question has been the nature of the iron-oxygen bond and, in particular, the protonation state. We present neutron structures of the ferric derivative of cytochrome c peroxidase and its ferryl intermediate; these allow direct visualization of protonation states. We demonstrate that the ferryl heme is an Fe(IV)=O species and is not protonated. Comparison of the structures shows that the distal histidine becomes protonated on formation of the ferryl intermediate, which has implications for the understanding of O-O bond cleavage in heme enzymes. The structures highlight the advantages of neutron cryo-crystallography in probing reaction mechanisms and visualizing protonation states in enzyme intermediates.
Heme enzymes. Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase.,Casadei CM, Gumiero A, Metcalfe CL, Murphy EJ, Basran J, Concilio MG, Teixeira SC, Schrader TE, Fielding AJ, Ostermann A, Blakeley MP, Raven EL, Moody PC Science. 2014 Jul 11;345(6193):193-7. doi: 10.1126/science.1254398. Epub 2014 Jul, 10. PMID:25013070[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Casadei CM, Gumiero A, Metcalfe CL, Murphy EJ, Basran J, Concilio MG, Teixeira SC, Schrader TE, Fielding AJ, Ostermann A, Blakeley MP, Raven EL, Moody PC. Heme enzymes. Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase. Science. 2014 Jul 11;345(6193):193-7. doi: 10.1126/science.1254398. Epub 2014 Jul, 10. PMID:25013070 doi:http://dx.doi.org/10.1126/science.1254398
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