1irv

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(New page: 200px<br /><applet load="1irv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1irv, resolution 1.9&Aring;" /> '''CYTOCHROME C ISOZYME ...)
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[[Image:1irv.gif|left|200px]]<br /><applet load="1irv" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1irv, resolution 1.9&Aring;" />
 
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'''CYTOCHROME C ISOZYME 1, REDUCED, MUTANT WITH ILE 75 REPLACED BY MET AND CYS 102 REPLACED BY THR'''<br />
 
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==Overview==
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==CYTOCHROME C ISOZYME 1, REDUCED, MUTANT WITH ILE 75 REPLACED BY MET AND CYS 102 REPLACED BY THR==
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The influence of mutations in two conserved regions of yeast, iso-1-cytochrome c believed to be critical to the mechanism of cytochrome, c electron transfer reactions has been investigated. The variants, Asn52Ala, Tyr67Phe, Ile75Met, and Thr78Gly involve perturbation of, critical hydrogen-bonding interactions with an internal water molecule, (Wat166) and have been studied in terms of their electrochemical, properties and the kinetics with which they are reduced by Fe(EDTA)2- and, oxidized by Co(phen)3(3+). In parallel studies, the Co(phen)3(3+), oxidation kinetics of Tyr, Leu, Ile, Ala, Ser, and Gly variants of the, phylogenetically conserved residue Phe82 have been studied and correlated, with previous electrochemical and kinetic results. To assist mechanistic, interpretation of these results, the three-dimensional structures of the, Asn52Ala and Ile75Met ferrocytochrome c variants have been determined. The, reduction potentials of the variants modified in the region of Wat166 were, at least 33 mV (pH 6, 25 degrees C, and mu = 0.1 M) lower than that of the, wild-type protein. Electron transfer reactivity of this family of variants, in both the oxidation and reduction reactions was increased as much as, 10-fold over that of the wild-type cytochrome. On the other hand, the, reactivity of the position-82 variants in both oxidation and reduction, depended on the structural characteristics of the oxidation-reduction, reagent with which they reacted, and this reactivity was related to the, nature of the residue at this position. These findings have been, interpreted as demonstrating that the principal influence of modification, at position-82 arises from changes in the nature of reactant-protein, interaction at the surface of the protein and in maintaining the high, reduction potential of the cytochrome while the principal influence of, internal modifications near Wat166 results from alteration of the, reorganization energy for the oxidation state-linked conformational change, defined by crystallographic analysis of the wild-type protein.
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<StructureSection load='1irv' size='340' side='right'caption='[[1irv]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1irv]] 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=1IRV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IRV 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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1irv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1irv OCA], [https://pdbe.org/1irv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1irv RCSB], [https://www.ebi.ac.uk/pdbsum/1irv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1irv 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/ir/1irv_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=1irv 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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1IRV 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 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=1IRV 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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Mechanistic and structural contributions of critical surface and internal residues to cytochrome c electron transfer reactivity., Rafferty SP, Guillemette JG, Berghuis AM, Smith M, Brayer GD, Mauk AG, Biochemistry. 1996 Aug 20;35(33):10784-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8718869 8718869]
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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: electron transport]]
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[[Category: heme protein]]
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[[Category: mitochondrion]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:36:56 2007''
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Current revision

CYTOCHROME C ISOZYME 1, REDUCED, MUTANT WITH ILE 75 REPLACED BY MET AND CYS 102 REPLACED BY THR

PDB ID 1irv

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