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3wui

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Revision as of 07:51, 4 August 2016

Dimeric horse cytochrome c formed by refolding from molten globule state

Structural highlights

3wui is a 1 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:	, , ,
Related:	3wc8
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

Many proteins, including cytochrome c (cyt c), have been shown to form domain-swapped oligomers, but the factors governing the oligomerization process remain unrevealed. We obtained oligomers of cyt c by refolding cyt c from its acid molten globule state to neutral pH state under high protein and ion concentrations. The amount of oligomeric cyt c obtained depended on the nature of the anion (chaotropic or kosmotropic) in the solution: ClO4- (oligomers, 11% +/- 2% (heme unit)), SCN- (10% +/- 2%), I- (6% +/- 2%), NO3- (3% +/- 1%), Br- (2% +/- 1%), Cl- (2% +/- 1%), and SO42- (3% +/- 1%) for refolding of 2 mM cyt c (anion concentration 125 mM). Dimeric cyt c obtained by refolding from the molten globule state exhibited a domain-swapped structure, in which the C-terminal alpha-helices were exchanged between protomers. According to small-angle X-ray scattering measurements, approximately 25% of the cyt c molecules were dimerized in the molten globule state containing 125 mM ClO4-. These results indicate that a certain amount of molten globule state oligomers of cyt c convert to domain-swapped oligomers during refolding and that the intermolecular interactions necessary for domain swapping are present in the molten globule state.

Formation of Domain-Swapped Oligomer of Cytochrome c from Its Molten Globule State Oligomer.,Deshpande MS, Parui PP, Kamikubo H, Yamanaka M, Nagao S, Komori H, Kataoka M, Higuchi Y, Hirota S Biochemistry. 2014 Jul 9. PMID:24981551^[1]

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

References

↑ Deshpande MS, Parui PP, Kamikubo H, Yamanaka M, Nagao S, Komori H, Kataoka M, Higuchi Y, Hirota S. Formation of Domain-Swapped Oligomer of Cytochrome c from Its Molten Globule State Oligomer. Biochemistry. 2014 Jul 9. PMID:24981551 doi:http://dx.doi.org/10.1021/bi500497s

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/3wui"

@@ Line 1: / Line 1: @@
 ==Dimeric horse cytochrome c formed by refolding from molten globule state==
 <StructureSection load='3wui' size='340' side='right' caption='[[3wui]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wc8|3wc8]]</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=3wui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wui OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wui RCSB], [http://www.ebi.ac.uk/pdbsum/3wui 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=3wui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wui OCA], [http://pdbe.org/3wui PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wui RCSB], [http://www.ebi.ac.uk/pdbsum/3wui PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wui ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3wui" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cytochrome c|Cytochrome c]]
 == References ==
 <references/>

3wui

From Proteopedia

Revision as of 07:51, 4 August 2016

Dimeric horse cytochrome c formed by refolding from molten globule state

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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