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1i55

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(New page: 200px<br /><applet load="1i55" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i55, resolution 2.00&Aring;" /> '''CYTOCHROME C (TUNA) ...)
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[[Image:1i55.gif|left|200px]]<br /><applet load="1i55" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1i55, resolution 2.00&Aring;" />
 
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'''CYTOCHROME C (TUNA) WITH 2ZN:1FE MIXED-METAL PORPHYRINS'''<br />
 
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==Overview==
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==CYTOCHROME C (TUNA) WITH 2ZN:1FE MIXED-METAL PORPHYRINS==
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The current understanding of electron tunneling through proteins has come, from work on systems where donors and acceptors are held at fixed, distances and orientations. The factors that control electron flow between, proteins are less well understood, owing to uncertainties in the relative, orientations and structures of the reactants during the very short time, that tunneling occurs. As we report here, the way around such structural, ambiguity is to examine oxidation-reduction reactions in protein crystals., Accordingly, we have measured and analyzed the kinetics of electron, transfer between native and Zn-substituted tuna cytochrome c (cyt c), molecules in crystals of known structure. Electron transfer rates [(320, s(-1) for *Zn-cyt c --&gt; Fe(III)-cyt c; 2000 s(-1) for Fe(II)-cyt c --&gt;, Zn-cyt c(+))] over a Zn-Fe distance of 24.1 A closely match those for, intraprotein electron tunneling over similar donor-acceptor separations., Our results indicate that van der Waals interactions and water-mediated, hydrogen bonds are effective coupling elements for tunneling across a, protein-protein interface.
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<StructureSection load='1i55' size='340' side='right'caption='[[1i55]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1i55]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thunnus_thynnus Thunnus thynnus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I55 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&#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=ZNH:PROTOPORPHYRIN+IX+CONTAINING+ZN'>ZNH</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=1i55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i55 OCA], [https://pdbe.org/1i55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i55 RCSB], [https://www.ebi.ac.uk/pdbsum/1i55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i55 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CYC_THUAA CYC_THUAA] 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/i5/1i55_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=1i55 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The current understanding of electron tunneling through proteins has come from work on systems where donors and acceptors are held at fixed distances and orientations. The factors that control electron flow between proteins are less well understood, owing to uncertainties in the relative orientations and structures of the reactants during the very short time that tunneling occurs. As we report here, the way around such structural ambiguity is to examine oxidation-reduction reactions in protein crystals. Accordingly, we have measured and analyzed the kinetics of electron transfer between native and Zn-substituted tuna cytochrome c (cyt c) molecules in crystals of known structure. Electron transfer rates [(320 s(-1) for *Zn-cyt c --&gt; Fe(III)-cyt c; 2000 s(-1) for Fe(II)-cyt c --&gt; Zn-cyt c(+))] over a Zn-Fe distance of 24.1 A closely match those for intraprotein electron tunneling over similar donor-acceptor separations. Our results indicate that van der Waals interactions and water-mediated hydrogen bonds are effective coupling elements for tunneling across a protein-protein interface.
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==About this Structure==
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Electron tunneling in protein crystals.,Tezcan FA, Crane BR, Winkler JR, Gray HB Proc Natl Acad Sci U S A. 2001 Apr 24;98(9):5002-6. Epub 2001 Apr 10. PMID:11296248<ref>PMID:11296248</ref>
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1I55 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thunnus_thynnus Thunnus thynnus] with HEM and ZNH as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I55 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Electron tunneling in protein crystals., Tezcan FA, Crane BR, Winkler JR, Gray HB, Proc Natl Acad Sci U S A. 2001 Apr 24;98(9):5002-6. Epub 2001 Apr 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11296248 11296248]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1i55" style="background-color:#fffaf0;"></div>
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[[Category: Thunnus thynnus]]
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[[Category: Crane, B.R.]]
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[[Category: Gray, H.B.]]
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[[Category: Tezcan, F.A.]]
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[[Category: Winkler, J.R.]]
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[[Category: HEM]]
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[[Category: ZNH]]
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[[Category: cytochrome c]]
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[[Category: electron transfer]]
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[[Category: zinc-porphyrin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:03:44 2007''
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==See Also==
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*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Thunnus thynnus]]
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[[Category: Crane BR]]
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[[Category: Gray HB]]
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[[Category: Tezcan FA]]
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[[Category: Winkler JR]]

Current revision

CYTOCHROME C (TUNA) WITH 2ZN:1FE MIXED-METAL PORPHYRINS

PDB ID 1i55

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