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1f22

From Proteopedia

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[[Image:1f22.jpg|left|200px]]
 
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{{Structure
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==A PROTON-NMR INVESTIGATION OF THE FULLY REDUCED CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS. COMPARISON BETWEEN THE REDUCED AND THE OXIDIZED FORMS.==
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|PDB= 1f22 |SIZE=350|CAPTION= <scene name='initialview01'>1f22</scene>
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<StructureSection load='1f22' size='340' side='right'caption='[[1f22]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=HEC:HEME C'>HEC</scene>
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<table><tr><td colspan='2'>[[1f22]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfuromonas_acetoxidans Desulfuromonas acetoxidans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F22 FirstGlance]. <br>
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|ACTIVITY=
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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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|GENE=
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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></td></tr>
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}}
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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=1f22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f22 OCA], [https://pdbe.org/1f22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f22 RCSB], [https://www.ebi.ac.uk/pdbsum/1f22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f22 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CYC3_DESAC CYC3_DESAC] Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin.
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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/f2/1f22_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=1f22 ConSurf].
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<div style="clear:both"></div>
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'''A PROTON-NMR INVESTIGATION OF THE FULLY REDUCED CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS. COMPARISON BETWEEN THE REDUCED AND THE OXIDIZED FORMS.'''
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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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The solution structure via 1H NMR of the fully reduced form of cytochrome c7 has been obtained. The protein sample was kept reduced by addition of catalytic amounts of Desulfovibrio gigas iron hydrogenase in H2 atmosphere after it had been checked that the presence of the hydrogenase did not affect the NMR spectrum. A final family of 35 conformers with rmsd values with respect to the mean structure of 8.7 +/- 1.5 nm and 12.4 +/- 1.3 nm for the backbone and heavy atoms, respectively, was obtained. A highly disordered loop involving residues 54-61 is present. If this loop is ignored, the rmsd values are 6.2 +/- 1.1 nm and 10.2 +/- 1.0 nm for the backbone and heavy atoms, respectively, which represent a reasonable resolution. The structure was analyzed and compared with the already available structure of the fully oxidized protein. Within the indetermination of the two solution structures, the result for the two redox forms is quite similar, confirming the special structural features of the three-heme cluster. A useful comparison can be made with the available crystal structures of cytochromes c3, which appear to be highly homologous except for the presence of a further heme. Finally, an analysis of the factors affecting the reduction potentials of the heme irons was performed, revealing the importance of net charges in differentiating the reduction potential when the other parameters are kept constant.
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==About this Structure==
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1F22 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Desulfuromonas_acetoxidans Desulfuromonas acetoxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F22 OCA].
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==Reference==
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A proton-NMR investigation of the fully reduced cytochrome c7 from Desulfuromonas acetoxidans. Comparison between the reduced and the oxidized forms., Assfalg M, Banci L, Bertini I, Bruschi M, Giudici-Orticoni MT, Turano P, Eur J Biochem. 1999 Dec;266(2):634-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10561607 10561607]
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[[Category: Desulfuromonas acetoxidans]]
[[Category: Desulfuromonas acetoxidans]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Assfalg, M.]]
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[[Category: Assfalg M]]
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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: Bruschi, M.]]
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[[Category: Bruschi M]]
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[[Category: Giudici-Orticoni, M T.]]
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[[Category: Giudici-Orticoni MT]]
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[[Category: HEC]]
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[[Category: triheme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:03:26 2008''
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Current revision

A PROTON-NMR INVESTIGATION OF THE FULLY REDUCED CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS. COMPARISON BETWEEN THE REDUCED AND THE OXIDIZED FORMS.

PDB ID 1f22

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