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1hrc

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(New page: 200px<br /><applet load="1hrc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hrc, resolution 1.9&Aring;" /> '''HIGH-RESOLUTION THREE...)
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[[Image:1hrc.gif|left|200px]]<br /><applet load="1hrc" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hrc, resolution 1.9&Aring;" />
 
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'''HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF HORSE HEART CYTOCHROME C'''<br />
 
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==Overview==
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==HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF HORSE HEART CYTOCHROME C==
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The 1.94 A resolution three-dimensional structure of oxidized horse heart, cytochrome c has been elucidated and refined to a final R-factor of 0.17., This has allowed for a detailed assessment of the structural features of, this protein, including the presence of secondary structure, hydrogen-bonding patterns and heme geometry. A comprehensive analysis of, the structural differences between horse heart cytochrome c and those, other eukaryotic cytochromes c for which high-resolution structures are, available (yeast iso-1, tuna, rice) has also been completed. Significant, conformational differences between these proteins occur in three regions, and primarily involve residues 22 to 27, 41 to 43 and 56 to 57. The first, of these variable regions is part of a surface beta-loop, whilst the, latter two are located together adjacent to the heme group. This study, also demonstrates that, in horse cytochrome c, the side-chain of Phe82 is, positioned in a co-planar fashion next to the heme in a conformation, comparable to that found in other cytochromes c. The positioning of this, residue does not therefore appear to be oxidation-state-dependent. In, total, five water molecules occupy conserved positions in the structures, of horse heart, yeast iso-1, tuna and rice cytochromes c. Three of these, are on the surface of the protein, serving to stabilize local polypeptide, chain conformations. The remaining two are internally located. One of, these mediates a charged interaction between the invariant residue Arg38, and a nearby heme propionate. The other is more centrally buried near the, heme iron atom and is hydrogen bonded to the conserved residues Asn52, Tyr67 and Thr78. It is shown that this latter water molecule shifts in a, consistent manner upon change in oxidation state if cytochrome c, structures from various sources are compared. The conservation of this, structural feature and its close proximity to the heme iron atom strongly, implicate this internal water molecule as having a functional role in the, mechanism of action of cytochrome c.
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<StructureSection load='1hrc' size='340' side='right'caption='[[1hrc]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hrc]] 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=1HRC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HRC 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">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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></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=1hrc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hrc OCA], [https://pdbe.org/1hrc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hrc RCSB], [https://www.ebi.ac.uk/pdbsum/1hrc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hrc 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/hr/1hrc_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=1hrc 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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1HRC 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 ACE and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HRC 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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High-resolution three-dimensional structure of horse heart cytochrome c., Bushnell GW, Louie GV, Brayer GD, J Mol Biol. 1990 Jul 20;214(2):585-95. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2166170 2166170]
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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: Brayer, G.D.]]
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[[Category: Brayer GD]]
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[[Category: Luo, Y.]]
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[[Category: Luo Y]]
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[[Category: ACE]]
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[[Category: HEM]]
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[[Category: electron transport(cytochrome)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:46:46 2007''
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HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF HORSE HEART CYTOCHROME C

PDB ID 1hrc

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