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==Crystal structure of Spider Monkey Cytochrome C at 1.15 Angstrom==
==Crystal structure of Spider Monkey Cytochrome C at 1.15 Angstrom==
<StructureSection load='5dfs' size='340' side='right' caption='[[5dfs]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
<StructureSection load='5dfs' size='340' side='right'caption='[[5dfs]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5dfs]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DFS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DFS FirstGlance]. <br>
<table><tr><td colspan='2'>[[5dfs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ateles_sp. Ateles sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DFS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DFS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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]] 1.15&#8491;</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=5dfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dfs OCA], [http://pdbe.org/5dfs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dfs RCSB], [http://www.ebi.ac.uk/pdbsum/5dfs PDBsum]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</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=5dfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dfs OCA], [https://pdbe.org/5dfs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dfs RCSB], [https://www.ebi.ac.uk/pdbsum/5dfs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dfs ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CYC_ATESP CYC_ATESP]] 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_ATESP CYC_ATESP] 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).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5dfs" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5dfs" style="background-color:#fffaf0;"></div>
==See Also==
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: BOWLER, B E]]
[[Category: Ateles sp]]
[[Category: Goldes, M E]]
[[Category: Large Structures]]
[[Category: Jeakins-Cooley, M E]]
[[Category: BOWLER BE]]
[[Category: MOU, T C]]
[[Category: Goldes ME]]
[[Category: McClelland, L J]]
[[Category: Jeakins-Cooley ME]]
[[Category: SPRANG, S R]]
[[Category: MOU TC]]
[[Category: Electron transport]]
[[Category: McClelland LJ]]
[[Category: Mitochondrial cytochrome c]]
[[Category: SPRANG SR]]
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