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5df5
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5df5 is ON HOLD until Paper Publication Authors: Edwards, B.F.P., Mahapatra, G., Vaishnav, A.A., Brunzelle, J.S., Huttemann, M. Description: [[Cat...) |
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The structure of oxidized rat cytochrome c (T28E) at 1.30 angstroms resolution.== |
| + | <StructureSection load='5df5' size='340' side='right'caption='[[5df5]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5df5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DF5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.301Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FC6:HEXACYANOFERRATE(3-)'>FC6</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=5df5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5df5 OCA], [https://pdbe.org/5df5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5df5 RCSB], [https://www.ebi.ac.uk/pdbsum/5df5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5df5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CYC_RAT CYC_RAT] 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== | |
| - | + | *[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | |
| - | + | __TOC__ | |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Huttemann | + | [[Category: Brunzelle JS]] |
| - | [[Category: | + | [[Category: Edwards BFP]] |
| - | [[Category: | + | [[Category: Huttemann M]] |
| + | [[Category: Mahapatra G]] | ||
| + | [[Category: Vaishnav AA]] | ||
Current revision
The structure of oxidized rat cytochrome c (T28E) at 1.30 angstroms resolution.
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