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| | <StructureSection load='2b4z' size='340' side='right'caption='[[2b4z]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='2b4z' size='340' side='right'caption='[[2b4z]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2b4z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B4Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2B4Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2b4z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B4Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 1.5Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b4z OCA], [http://pdbe.org/2b4z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b4z RCSB], [http://www.ebi.ac.uk/pdbsum/2b4z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2b4z ProSAT]</span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b4z OCA], [https://pdbe.org/2b4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b4z RCSB], [https://www.ebi.ac.uk/pdbsum/2b4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b4z ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CYC_BOVIN CYC_BOVIN]] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity). | + | [https://www.uniprot.org/uniprot/CYC_BOVIN CYC_BOVIN] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jakoncic, J]] | + | [[Category: Jakoncic J]] |
| - | [[Category: Mirkin, N]] | + | [[Category: Mirkin N]] |
| - | [[Category: Moreno, A]] | + | [[Category: Moreno A]] |
| - | [[Category: Stojanoff, V]] | + | [[Category: Stojanoff V]] |
| - | [[Category: Electron transport]]
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| - | [[Category: Ferric form]]
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| - | [[Category: Low ionic strength]]
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| Structural highlights
Function
CYC_BOVIN Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity).
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 is one of the most studied proteins probably due to its electron-transfer properties in aerobic and anaerobic respiration. Particularly, cytochrome c from bovine heart is a small protein, M(r) 12,230 Da, globular (hydrodynamic diameter of 3.4 nm), soluble in different buffer solutions, and commercially available. Despite being a quite well-studied protein and relatively easy to manipulate from the biochemical and electrochemical viewpoint, its 3D structure has never been published. In this work, the purification, crystallization and 3D structure of one of the cytochrome c isoforms is presented to 1.5 A resolution. It is also shown how the presence of isoforms made both the purification and crystallization steps difficult. Finally, a new approach for protein electrocrystallization and design of biosensors is presented.
High resolution X-ray crystallographic structure of bovine heart cytochrome c and its application to the design of an electron transfer biosensor.,Mirkin N, Jaconcic J, Stojanoff V, Moreno A Proteins. 2008 Jan 1;70(1):83-92. PMID:17634981[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mirkin N, Jaconcic J, Stojanoff V, Moreno A. High resolution X-ray crystallographic structure of bovine heart cytochrome c and its application to the design of an electron transfer biosensor. Proteins. 2008 Jan 1;70(1):83-92. PMID:17634981 doi:10.1002/prot.21452
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