4cvj
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Neutron Structure of Compound I intermediate of Cytochrome c Peroxidase - Deuterium exchanged 100 K== | |
| + | <StructureSection load='4cvj' size='340' side='right'caption='[[4cvj]], [[Resolution|resolution]] 2.18Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Hybrid , Neutron Diffraction , X-ray diffraction, [[Resolution|Resolution]] 2.182Å</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='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> | ||
| + | </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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:25013070</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4cvj" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae]] | ||
| + | [[Category: Blakeley MP]] | ||
| + | [[Category: Casadei CM]] | ||
| + | [[Category: Gumiero A]] | ||
| + | [[Category: Moody PCE]] | ||
| + | [[Category: Ostermann A]] | ||
| + | [[Category: Raven EL]] | ||
Current revision
Neutron Structure of Compound I intermediate of Cytochrome c Peroxidase - Deuterium exchanged 100 K
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