|
|
| Line 1: |
Line 1: |
|
| |
|
| ==Dimeric horse cytochrome c formed by refolding from molten globule state== | | ==Dimeric horse cytochrome c formed by refolding from molten globule state== |
| <StructureSection load='3wui' size='340' side='right'caption='[[3wui]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='3wui' size='340' side='right'caption='[[3wui]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3wui]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WUI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WUI FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WUI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WUI FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</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> | | </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=3wui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wui OCA], [https://pdbe.org/3wui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wui RCSB], [https://www.ebi.ac.uk/pdbsum/3wui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wui ProSAT]</span></td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3wc8|3wc8]]</div></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=3wui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wui OCA], [https://pdbe.org/3wui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wui RCSB], [https://www.ebi.ac.uk/pdbsum/3wui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wui ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function ==
| |
| [[https://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 ==
| |
| 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<ref>PMID:24981551</ref>
| |
|
| |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| |
| </div>
| |
| <div class="pdbe-citations 3wui" style="background-color:#fffaf0;"></div>
| |
|
| |
|
| ==See Also== | | ==See Also== |
| *[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | | *[[Cytochrome C 3D structures|Cytochrome C 3D structures]] |
| == References ==
| |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Equus caballus]]
| |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Deshpande, M S]] | | [[Category: Deshpande MS]] |
| [[Category: Higuchi, Y]] | | [[Category: Higuchi Y]] |
| [[Category: Hirota, S]] | | [[Category: Hirota S]] |
| [[Category: Kamikubo, H]] | | [[Category: Kamikubo H]] |
| [[Category: Kataoka, M]] | | [[Category: Kataoka M]] |
| [[Category: Komori, H]] | | [[Category: Komori H]] |
| [[Category: Nagao, S]] | | [[Category: Nagao S]] |
| [[Category: Parui, P P]] | | [[Category: Parui PP]] |
| [[Category: Yamanaka, M]] | | [[Category: Yamanaka M]] |
| [[Category: Electron transport]]
| |
