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1cty

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(New page: 200px<br /><applet load="1cty" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cty, resolution 2.2&Aring;" /> '''MUTATION OF TYROSINE-...)
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[[Image:1cty.jpg|left|200px]]<br /><applet load="1cty" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cty, resolution 2.2&Aring;" />
 
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'''MUTATION OF TYROSINE-67 IN CYTOCHROME C SIGNIFICANTLY ALTERS THE LOCAL HEME ENVIRONMENT'''<br />
 
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==Overview==
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==MUTATION OF TYROSINE-67 IN CYTOCHROME C SIGNIFICANTLY ALTERS THE LOCAL HEME ENVIRONMENT==
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The high resolution three-dimensional atomic structures of the reduced and, oxidized states of the Y67F variant of yeast iso-1-cytochrome c have been, completed. The conformational differences observed are localized directly, in the mutation site and in the region about the pyrrole A propionate., Shifts in atomic positions are largely restricted to nearby amino acid, side-chains, whereas little perturbation of the polypeptide chain backbone, is observed. One prominent difference between the variant and wild-type, structures involves a substantial increase in the size of an already, existing internal cavity adjacent to residue 67. This same cavity contains, an internally bound water molecule (Wat166), which is found in all, eukaryotic cytochromes c for which structures are available. In the, reduced Y67F mutant protein a second water molecule (Wat300) is observed, to reside in this enlarged internal cavity, assuming a position, approximately equivalent to that of the hydroxyl group of Tyr67 in the, wild-type protein. A further consequence of this mutation is the, alteration of the hydrogen bond network between Tyr67, Wat166 and other, nearby residues. This appears to be responsible for the absence of, oxidation state dependent changes in polypeptide chain flexibility, observed in the wild-type protein. Furthermore, loss of the normally, resident Tyr67 OH to Met80 SD hydrogen bond leads to a significantly lower, midpoint reduction potential. These results reaffirm proposals that both, Tyr67 and Wat166 play a central role in stabilizing the alternative, oxidation states of cytochrome c.
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<StructureSection load='1cty' size='340' side='right'caption='[[1cty]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cty]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CTY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CTY 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]] 2.2&#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=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1cty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cty OCA], [https://pdbe.org/1cty PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cty RCSB], [https://www.ebi.ac.uk/pdbsum/1cty PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cty ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CYC1_YEAST CYC1_YEAST] 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.
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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/ct/1cty_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=1cty 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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1CTY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4, HEM and TML as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CTY 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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Mutation of tyrosine-67 to phenylalanine in cytochrome c significantly alters the local heme environment., Berghuis AM, Guillemette JG, Smith M, Brayer GD, J Mol Biol. 1994 Jan 28;235(4):1326-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8308895 8308895]
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Berghuis AM]]
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[[Category: Berghuis, A.M.]]
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[[Category: Brayer GD]]
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[[Category: Brayer, G.D.]]
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[[Category: HEM]]
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[[Category: SO4]]
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[[Category: TML]]
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[[Category: electron transport (heme protein)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:45:32 2007''
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Current revision

MUTATION OF TYROSINE-67 IN CYTOCHROME C SIGNIFICANTLY ALTERS THE LOCAL HEME ENVIRONMENT

PDB ID 1cty

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