3o20
From Proteopedia
(Difference between revisions)
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| - | + | ==Electron transfer complexes:experimental mapping of the Redox-dependent Cytochrome C electrostatic surface== | |
| - | + | <StructureSection load='3o20' size='340' side='right' caption='[[3o20]], [[Resolution|resolution]] 1.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3o20]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O20 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O20 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | |
| - | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kyo|1kyo]], [[2pcc|2pcc]], [[2pcb|2pcb]], [[1l9j|1l9j]]</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=3o20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o20 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o20 RCSB], [http://www.ebi.ac.uk/pdbsum/3o20 PDBsum]</span></td></tr> |
| - | [[3o20]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O20 OCA]. | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/CYC_HORSE CYC_HORSE]] 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). | ||
==See Also== | ==See Also== | ||
*[[Cytochrome c|Cytochrome c]] | *[[Cytochrome c|Cytochrome c]] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
| - | [[Category: Casini, A | + | [[Category: Casini, A]] |
| - | [[Category: Demitri, N | + | [[Category: Demitri, N]] |
| - | [[Category: Gabbiani, C | + | [[Category: Gabbiani, C]] |
| - | [[Category: Geremia, S | + | [[Category: Geremia, S]] |
| - | [[Category: Guerri, A | + | [[Category: Guerri, A]] |
| - | [[Category: March, M De | + | [[Category: March, M De]] |
| - | [[Category: Messori, L | + | [[Category: Messori, L]] |
| - | [[Category: Zorzi, R De | + | [[Category: Zorzi, R De]] |
[[Category: Electron carrier]] | [[Category: Electron carrier]] | ||
[[Category: Electron transport]] | [[Category: Electron transport]] | ||
Revision as of 18:58, 24 December 2014
Electron transfer complexes:experimental mapping of the Redox-dependent Cytochrome C electrostatic surface
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