1gx7
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(New page: 200px<br /><applet load="1gx7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gx7" /> '''BEST MODEL OF THE ELECTRON TRANSFER COMPLEX ...) |
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| - | [[Image:1gx7.gif|left|200px]]<br /><applet load="1gx7" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1gx7" /> | ||
| - | '''BEST MODEL OF THE ELECTRON TRANSFER COMPLEX BETWEEN CYTOCHROME C3 AND [FE]-HYDROGENASE'''<br /> | ||
| - | == | + | ==Best model of the electron transfer complex between cytochrome c3 and [Fe]-hydrogenase== |
| - | Cytochrome c(3) (M(r) 13000) is a low redox potential cytochrome specific | + | <StructureSection load='1gx7' size='340' side='right'caption='[[1gx7]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1gx7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_vulgaris_str._Hildenborough Desulfovibrio vulgaris str. Hildenborough]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GX7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GX7 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Hybrid , Solution NMR , Theoretical Model, 1 model</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=PDT:1,3-PROPANEDITHIOL'>PDT</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gx7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gx7 OCA], [https://pdbe.org/1gx7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gx7 RCSB], [https://www.ebi.ac.uk/pdbsum/1gx7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gx7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PHFL_NITV2 PHFL_NITV2] May be involved in hydrogen uptake for the reduction of sulfate to hydrogen sulfide in an electron transport chain. Cytochrome c3 is likely to be the physiological electron carrier for the enzyme. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gx/1gx7_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1gx7 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cytochrome c(3) (M(r) 13000) is a low redox potential cytochrome specific of the anaerobic metabolism in sulfate-reducing bacteria. This tetrahemic cytochrome is an intermediate between the [Fe]-hydrogenase and the cytochrome Hmc in Desulfovibrio vulgaris Hildenborough strain. The present work describes the structural model of the cytochrome c(3)-[Fe]-hydrogenase complex obtained by nuclear magnetic resonance restrained docking. This model connects the distal cluster of the [Fe]-hydrogenase to heme 4 of the cytochrome, the same heme found in the interaction with cytochrome Hmc. This result gives evidence that cytochrome c(3) is an electron shuttle between the periplasmic hydrogenase and the Hmc membrane-bound complex. | ||
| - | + | The cytochrome c3-[Fe]-hydrogenase electron-transfer complex: structural model by NMR restrained docking.,ElAntak L, Morelli X, Bornet O, Hatchikian C, Czjzek M, Dolla A, Guerlesquin F FEBS Lett. 2003 Jul 31;548(1-3):1-4. PMID:12885397<ref>PMID:12885397</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1gx7" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Desulfovibrio vulgaris str. Hildenborough]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bornet O]] | ||
| + | [[Category: Czjzek M]] | ||
| + | [[Category: Dolla A]] | ||
| + | [[Category: Elantak L]] | ||
| + | [[Category: Guerlesquin F]] | ||
| + | [[Category: Hatchikian C]] | ||
| + | [[Category: Morelli X]] | ||
Current revision
Best model of the electron transfer complex between cytochrome c3 and [Fe]-hydrogenase
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