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3o1y

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Current revision (09:25, 6 September 2023) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3o1y]] is a 3 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=3O1Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O1Y FirstGlance]. <br>
<table><tr><td colspan='2'>[[3o1y]] is a 3 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=3O1Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O1Y FirstGlance]. <br>
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</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=NO3:NITRATE+ION'>NO3</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
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<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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1kyo|1kyo]], [[2pcc|2pcc]], [[2pcb|2pcb]], [[1l9j|1l9j]]</div></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3o1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o1y OCA], [https://pdbe.org/3o1y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o1y RCSB], [https://www.ebi.ac.uk/pdbsum/3o1y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o1y ProSAT]</span></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=3o1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o1y OCA], [https://pdbe.org/3o1y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o1y RCSB], [https://www.ebi.ac.uk/pdbsum/3o1y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o1y ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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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[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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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Casini, A]]
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[[Category: Casini A]]
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[[Category: Demitri, N]]
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[[Category: De March M]]
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[[Category: Gabbiani, C]]
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[[Category: De Zorzi R]]
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[[Category: Geremia, S]]
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[[Category: Demitri N]]
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[[Category: Guerri, A]]
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[[Category: Gabbiani C]]
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[[Category: March, M De]]
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[[Category: Geremia S]]
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[[Category: Messori, L]]
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[[Category: Guerri A]]
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[[Category: Zorzi, R De]]
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[[Category: Messori L]]
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[[Category: Cytochrome c]]
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[[Category: Electron carrier]]
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[[Category: Electron transport]]
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[[Category: Electron transport chain]]
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[[Category: Globular protein]]
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[[Category: Mitochondrial respiration]]
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Current revision

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

PDB ID 3o1y

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