3o1y

From Proteopedia

(Difference between revisions)

Revision as of 08:12, 5 August 2016

Electron transfer complexes: Experimental mapping of the redox-dependent cytochrome c electrostatic surface

Structural highlights

3o1y is a 3 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Related:	1kyo, 2pcc, 2pcb, 1l9j
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Schafer E, Dencher NA, Vonck J, Parcej DN. Three-dimensional structure of the respiratory chain supercomplex I1III2IV1 from bovine heart mitochondria. Biochemistry. 2007 Nov 6;46(44):12579-85. Epub 2007 Oct 10. PMID:17927210 doi:10.1021/bi700983h

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3o1y"

@@ Line 1: / Line 1: @@
 ==Electron transfer complexes: Experimental mapping of the redox-dependent cytochrome c electrostatic surface==
 <StructureSection load='3o1y' size='340' side='right' caption='[[3o1y]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <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>
+<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://pdbe.org/3o1y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o1y RCSB], [http://www.ebi.ac.uk/pdbsum/3o1y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o1y ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3o1y" style="background-color:#fffaf0;"></div>
 ==See Also==

3o1y

From Proteopedia

Revision as of 08:12, 5 August 2016

Electron transfer complexes: Experimental mapping of the redox-dependent cytochrome c electrostatic surface

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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