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| | <StructureSection load='1zbz' size='340' side='right'caption='[[1zbz]], [[Resolution|resolution]] 1.29Å' scene=''> | | <StructureSection load='1zbz' size='340' side='right'caption='[[1zbz]], [[Resolution|resolution]] 1.29Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zbz]] 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=1ZBZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1ZBZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1zbz]] 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=1ZBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZBZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]] 1.29Å</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]], [[1kok|1kok]], [[1z53|1z53]], [[1zby|1zby]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CCP1 ([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=1zbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zbz OCA], [https://pdbe.org/1zbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zbz RCSB], [https://www.ebi.ac.uk/pdbsum/1zbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zbz 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=1zbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zbz OCA], [http://pdbe.org/1zbz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zbz RCSB], [http://www.ebi.ac.uk/pdbsum/1zbz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zbz 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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| - | [[Category: Cytochrome-c peroxidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bhaskar, B]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Bonagura, C A]] | + | [[Category: Bhaskar B]] |
| - | [[Category: Goodin, D B]] | + | [[Category: Bonagura CA]] |
| - | [[Category: Li, H]] | + | [[Category: Goodin DB]] |
| - | [[Category: McRee, D E]] | + | [[Category: Li H]] |
| - | [[Category: Poulos, T L]] | + | [[Category: McRee DE]] |
| - | [[Category: Shimizu, H]] | + | [[Category: Poulos TL]] |
| - | [[Category: Sundaramoorthy, M]] | + | [[Category: Shimizu H]] |
| - | [[Category: Ccp]]
| + | [[Category: Sundaramoorthy M]] |
| - | [[Category: Heme peroxidase]]
| + | |
| - | [[Category: High-spin heme]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Trp191 cation radical]]
| + | |
| Structural highlights
Function
CCPR_YEAST Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Cytochrome c peroxidase (CCP) is a 32.5 kDa mitochondrial intermembrane space heme peroxidase from Saccharomyces cerevisiae that reduces H(2)O(2) to 2H(2)O by oxidizing two molecules of cytochrome c (cyt c). Here we compare the 1.2 A native structure (CCP) with the 1.3 A structure of its stable oxidized reaction intermediate, Compound I (CCP1). In addition, crystals were analyzed by UV-vis absorption and electron paramagnetic resonance spectroscopies before and after data collection to determine the state of the Fe(IV) center and the cationic Trp191 radical formed in Compound I. The results show that X-ray exposure does not lead to reduction of Fe(IV) and only partial reduction of the Trp radical. A comparison of the two structures reveals subtle but important conformational changes that aid in the stabilization of the Trp191 cationic radical in Compound I. The higher-resolution data also enable a more accurate determination of changes in heme parameters. Most importantly, when one goes from resting state Fe(III) to Compound I, the His-Fe bond distance increases, the iron moves into the porphyrin plane leading to shorter pyrrole N-Fe bonds, and the Fe(IV)-O bond distance is 1.87 A, suggesting a single Fe(IV)-O bond and not the generally accepted double bond.
High-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase.,Bonagura CA, Bhaskar B, Shimizu H, Li H, Sundaramoorthy M, McRee DE, Goodin DB, Poulos TL Biochemistry. 2003 May 20;42(19):5600-8. PMID:12741816[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bonagura CA, Bhaskar B, Shimizu H, Li H, Sundaramoorthy M, McRee DE, Goodin DB, Poulos TL. High-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase. Biochemistry. 2003 May 20;42(19):5600-8. PMID:12741816 doi:10.1021/bi034058c
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