5zkv: Difference between revisions
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==Solution structure of molten globule state of L94G mutant of horse cytochrome-c== | ==Solution structure of molten globule state of L94G mutant of horse cytochrome-c== | ||
<StructureSection load='5zkv' size='340' side='right'caption='[[5zkv | <StructureSection load='5zkv' size='340' side='right'caption='[[5zkv]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5zkv]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5zkv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZKV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZKV FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 15 models</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5zkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zkv OCA], [https://pdbe.org/5zkv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zkv RCSB], [https://www.ebi.ac.uk/pdbsum/5zkv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zkv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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). | ||
==See Also== | ==See Also== | ||
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[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ahmad | [[Category: Ahmad F]] | ||
[[Category: Hassan | [[Category: Hassan MI]] | ||
[[Category: Islam | [[Category: Islam A]] | ||
[[Category: Naiyer | [[Category: Naiyer A]] | ||
[[Category: Sundd | [[Category: Sundd M]] | ||
Latest revision as of 14:00, 30 October 2024
Solution structure of molten globule state of L94G mutant of horse cytochrome-cSolution structure of molten globule state of L94G mutant of horse cytochrome-c
Structural highlights
FunctionCYC_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). See Also |
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