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1m60

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(New page: 200px<br /><applet load="1m60" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m60" /> '''Solution Structure of Zinc-substituted cytoc...)
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[[Image:1m60.gif|left|200px]]<br /><applet load="1m60" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1m60" />
 
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'''Solution Structure of Zinc-substituted cytochrome c'''<br />
 
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==Overview==
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==Solution Structure of Zinc-substituted cytochrome c==
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Zinc-substituted cytochrome c has been widely used in studies of, protein-protein interactions and photo-induced electron transfer reactions, between proteins. However, the coordination geometry of zinc in, zinc-substituted cyt c has not yet been determined; two different opinions, about the coordination have been reached. Here the solution structures of, zinc-substituted cytochrome c that might be five-coordinated and, six-coordinated have been refined separately by using (1)H NMR, spectroscopy, and the zinc coordination geometry was determined just by, NOE distance constraints. Structural analysis of the energy-minimized, average solution structures of both the pentacoordinated and, hexacoordinated geometries indicate that that zinc in zinc-substituted cyt, c should be bound to both His18 and Met80, which means that the zinc is, six-coordinated. RMSD values of the family of 25 six-coordinated, structures from the average structure are 0.66+/-0.13 A and 1.09+/-0.16 A, for the backbone and all heavy atoms, respectively. A statistical analysis, of the structure indicates its satisfactory quality. Comparison of the, solution structure of the six-coordinated energy-minimized average, structure of zinc-substituted cytochrome c with the solution structure of, reduced cytochrome c reveals that for the overall folding the secondary, structure elements are very close. The availability of the structure, provides for a better understanding of the protein-protein complex and for, electron transfer processes between Zn cyt c and other metalloproteins.
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<StructureSection load='1m60' size='340' side='right'caption='[[1m60]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1m60]] 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=1M60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M60 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=HES:ZINC+SUBSTITUTED+HEME+C'>HES</scene></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=1m60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m60 OCA], [https://pdbe.org/1m60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m60 RCSB], [https://www.ebi.ac.uk/pdbsum/1m60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m60 ProSAT]</span></td></tr>
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</table>
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== 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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m6/1m60_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m60 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1M60 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with HES as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M60 OCA].
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*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structural analysis of zinc-substituted cytochrome c., Qian C, Yao Y, Tong Y, Wang J, Tang W, J Biol Inorg Chem. 2003 Apr;8(4):394-400. Epub 2002 Dec 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12761660 12761660]
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[[Category: Equus caballus]]
[[Category: Equus caballus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Qian, C.]]
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[[Category: Qian C]]
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[[Category: Tang, W.]]
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[[Category: Tang W]]
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[[Category: Tong, Y.]]
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[[Category: Tong Y]]
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[[Category: Wang, J.]]
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[[Category: Wang J]]
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[[Category: Yao, Y.]]
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[[Category: Yao Y]]
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[[Category: HES]]
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[[Category: six-coordinated zinc cyt c]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:10:25 2007''
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Current revision

Solution Structure of Zinc-substituted cytochrome c

PDB ID 1m60

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