3wui

<StructureSection load='3wui' size='340' side='right'caption='[[3wui]], [[Resolution|resolution]] 1.80&Aring;' scene=''>

<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>

</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>

<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>

== 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).

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3wui" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Equus caballus]]

[[Category: Deshpande, M S]]

[[Category: Higuchi, Y]]

[[Category: Hirota, S]]

[[Category: Kamikubo, H]]

[[Category: Kataoka, M]]

[[Category: Komori, H]]

[[Category: Nagao, S]]

[[Category: Parui, P P]]

[[Category: Yamanaka, M]]

[[Category: Electron transport]]