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1fi9

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[[Image:1fi9.gif|left|200px]]
 
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==SOLUTION STRUCTURE OF THE IMIDAZOLE COMPLEX OF CYTOCHROME C==
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The line below this paragraph, containing "STRUCTURE_1fi9", creates the "Structure Box" on the page.
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<StructureSection load='1fi9' size='340' side='right'caption='[[1fi9]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1fi9]] 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=1FI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FI9 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>
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{{STRUCTURE_1fi9| PDB=1fi9 | SCENE= }}
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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=1fi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fi9 OCA], [https://pdbe.org/1fi9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fi9 RCSB], [https://www.ebi.ac.uk/pdbsum/1fi9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fi9 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/fi/1fi9_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=1fi9 ConSurf].
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<div style="clear:both"></div>
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'''SOLUTION STRUCTURE OF THE IMIDAZOLE COMPLEX OF CYTOCHROME C'''
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==See Also==
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*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Although imidazole ligand binding to cytochrome c is not directly related to its physiological function, it has the potential to provide valuable information on the molecular and electronic structure of the protein. The solution structure of the imidazole adduct of oxidized horse heart cytochrome c (Im-cyt c) has been determined through 2D NMR spectroscopy. The Im-cyt c, 8 mM in 1.2 M imidazole solution at pH 5.7 and 313 K, provided altogether 2,542 NOEs (1,901 meaningful NOEs) and 194 pseudocontact shifts. The 35 conformers of the family show the RMSD values to the average structure of 0.063+/-0.007 nm for the backbone and 0.107+/-0.007 nm for all heavy atoms, respectively. The characterization of Im-cyt c is discussed in detail both in terms of structure and electronic properties. The replacement of the axial ligand Met80 with the exogenous imidazole ligand induces significant conformation changes in both backbone and side chains of the residues located in the distal axial ligand regions. The imidazole ligand binds essentially parallel to the imidazole of the proximal histidine, the two planes forming an angle of 8+/-7 degrees. The electron delocalization on the heme moiety and the magnetic susceptibility tensor are consistent with these structural features.
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==About this Structure==
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1FI9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FI9 OCA].
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==Reference==
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Effects of extrinsic imidazole ligation on the molecular and electronic structure of cytochrome c., Banci L, Bertini I, Liu G, Lu J, Reddig T, Tang W, Wu Y, Yao Y, Zhu D, J Biol Inorg Chem. 2001 Jun;6(5-6):628-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11472026 11472026]
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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: Banci, L.]]
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[[Category: Banci L]]
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[[Category: Bertini, I.]]
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[[Category: Bertini I]]
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[[Category: Liu, G.]]
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[[Category: Liu G]]
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[[Category: Lu, J.]]
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[[Category: Lu J]]
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[[Category: Reddig, T.]]
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[[Category: Reddig T]]
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[[Category: Tang, W.]]
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[[Category: Tang W]]
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[[Category: Wu, Y.]]
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[[Category: Wu Y]]
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[[Category: Zhu, D.]]
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[[Category: Zhu D]]
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[[Category: Cytochrome c]]
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[[Category: Nmr]]
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[[Category: Solution structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:21:35 2008''
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Current revision

SOLUTION STRUCTURE OF THE IMIDAZOLE COMPLEX OF CYTOCHROME C

PDB ID 1fi9

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