3o1y: Difference between revisions
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[[ | ==Electron transfer complexes: Experimental mapping of the redox-dependent cytochrome c electrostatic surface== | ||
<StructureSection load='3o1y' size='340' side='right' caption='[[3o1y]], [[Resolution|resolution]] 1.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3o1y]] 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=3O1Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O1Y 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=3o1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o1y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o1y RCSB], [http://www.ebi.ac.uk/pdbsum/3o1y PDBsum]</span></td></tr> | |||
</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). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The respiratory chain complexes can arrange into multienzyme assemblies, so-called supercomplexes. We present the first 3D map of a respiratory chain supercomplex. It was determined by random conical tilt electron microscopy analysis of a bovine supercomplex consisting of complex I, dimeric complex III, and complex IV (I1III2IV1). Within this 3D map the positions and orientations of all the individual complexes in the supercomplex were determined unambiguously. Furthermore, the ubiquinone and cytochrome c binding sites of each complex in the supercomplex could be located. The mobile electron carrier binding site of each complex was found to be in proximity to the binding site of the succeeding complex in the respiratory chain. This provides structural evidence for direct substrate channeling in the supercomplex assembly with short diffusion distances for the mobile electron carriers. | |||
Three-dimensional structure of the respiratory chain supercomplex I1III2IV1 from bovine heart mitochondria.,Schafer E, Dencher NA, Vonck J, Parcej DN Biochemistry. 2007 Nov 6;46(44):12579-85. Epub 2007 Oct 10. PMID:17927210<ref>PMID:17927210</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Cytochrome c|Cytochrome c]] | *[[Cytochrome c|Cytochrome c]] | ||
== References == | |||
== | <references/> | ||
< | __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: Cytochrome c]] | [[Category: Cytochrome c]] | ||
[[Category: Electron carrier]] | [[Category: Electron carrier]] | ||
Revision as of 20:10, 25 December 2014
Electron transfer complexes: Experimental mapping of the redox-dependent cytochrome c electrostatic surfaceElectron transfer complexes: Experimental mapping of the redox-dependent cytochrome c electrostatic surface
Structural highlights
Function[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). Publication Abstract from PubMedThe respiratory chain complexes can arrange into multienzyme assemblies, so-called supercomplexes. We present the first 3D map of a respiratory chain supercomplex. It was determined by random conical tilt electron microscopy analysis of a bovine supercomplex consisting of complex I, dimeric complex III, and complex IV (I1III2IV1). Within this 3D map the positions and orientations of all the individual complexes in the supercomplex were determined unambiguously. Furthermore, the ubiquinone and cytochrome c binding sites of each complex in the supercomplex could be located. The mobile electron carrier binding site of each complex was found to be in proximity to the binding site of the succeeding complex in the respiratory chain. This provides structural evidence for direct substrate channeling in the supercomplex assembly with short diffusion distances for the mobile electron carriers. Three-dimensional structure of the respiratory chain supercomplex I1III2IV1 from bovine heart mitochondria.,Schafer E, Dencher NA, Vonck J, Parcej DN Biochemistry. 2007 Nov 6;46(44):12579-85. Epub 2007 Oct 10. PMID:17927210[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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