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[[Image:1i77.gif|left|200px]]
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{{STRUCTURE_1i77|  PDB=1i77  |  SCENE=  }}
'''CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ESSEX 6'''


==CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ESSEX 6==
<StructureSection load='1i77' size='340' side='right'caption='[[1i77]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1i77]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I77 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
<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></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=1i77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i77 OCA], [https://pdbe.org/1i77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i77 RCSB], [https://www.ebi.ac.uk/pdbsum/1i77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i77 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9L915_DESDE Q9L915_DESDE]
== 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/i7/1i77_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=1i77 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cytochrome c3, a small (14-kDa) soluble tetraheme protein was isolated from the periplasmic fraction of Desulfovibrio desulfuricans strain Essex 6. Its major physiological function appears to be that of an electron carrier for the periplasmic hydrogenase. It has been also shown to interact with the high-molecular-mass cytochrome complex in the cytoplasmic membrane, which eventually feeds electrons into the membraneous quinone pool, as well as with the membrane-associated dissimilatory sulfite reductase. The EPR spectra show features of four different low-spin Fe(III) hemes. Orthorhombic crystals of cytochrome c3 were obtained and X-ray diffraction data were collected to below 2 A resolution. The structure was solved by molecular replacement using cytochrome c3 from D. desulfuricans ATCC 27774 as a search model.


==Overview==
Spectroscopic investigation and determination of reactivity and structure of the tetraheme cytochrome c3 from Desulfovibrio desulfuricans Essex 6.,Einsle O, Foerster S, Mann K, Fritz G, Messerschmidt A, Kroneck PM Eur J Biochem. 2001 May;268(10):3028-35. PMID:11358521<ref>PMID:11358521</ref>
Cytochrome c3, a small (14-kDa) soluble tetraheme protein was isolated from the periplasmic fraction of Desulfovibrio desulfuricans strain Essex 6. Its major physiological function appears to be that of an electron carrier for the periplasmic hydrogenase. It has been also shown to interact with the high-molecular-mass cytochrome complex in the cytoplasmic membrane, which eventually feeds electrons into the membraneous quinone pool, as well as with the membrane-associated dissimilatory sulfite reductase. The EPR spectra show features of four different low-spin Fe(III) hemes. Orthorhombic crystals of cytochrome c3 were obtained and X-ray diffraction data were collected to below 2 A resolution. The structure was solved by molecular replacement using cytochrome c3 from D. desulfuricans ATCC 27774 as a search model.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1I77 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I77 OCA].
</div>
<div class="pdbe-citations 1i77" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Spectroscopic investigation and determination of reactivity and structure of the tetraheme cytochrome c3 from Desulfovibrio desulfuricans Essex 6., Einsle O, Foerster S, Mann K, Fritz G, Messerschmidt A, Kroneck PM, Eur J Biochem. 2001 May;268(10):3028-35. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11358521 11358521]
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Desulfovibrio desulfuricans]]
[[Category: Desulfovibrio desulfuricans]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Einsle, O.]]
[[Category: Einsle O]]
[[Category: Foerster, S.]]
[[Category: Foerster S]]
[[Category: Fritz, G.]]
[[Category: Fritz G]]
[[Category: Kroneck, P M.H.]]
[[Category: Kroneck PMH]]
[[Category: Mann, K H.]]
[[Category: Mann KH]]
[[Category: Messerschmidt, A.]]
[[Category: Messerschmidt A]]
[[Category: Multi-heme cytochrome c]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:39:28 2008''

Latest revision as of 06:08, 13 August 2026

CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ESSEX 6

1i77, resolution 1.95Å

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