1new
From Proteopedia
(Difference between revisions)
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==Cytochrome C551.5, NMR== | ==Cytochrome C551.5, NMR== | ||
- | <StructureSection load='1new' size='340' side='right'caption='[[1new | + | <StructureSection load='1new' size='340' side='right'caption='[[1new]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1new]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfuromonas_acetoxidans Desulfuromonas acetoxidans]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2new 2new] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cfo 1cfo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NEW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NEW FirstGlance]. <br> | <table><tr><td colspan='2'>[[1new]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfuromonas_acetoxidans Desulfuromonas acetoxidans]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2new 2new] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cfo 1cfo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NEW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NEW FirstGlance]. <br> | ||
- | </td></tr><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
+ | <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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1new FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1new OCA], [https://pdbe.org/1new PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1new RCSB], [https://www.ebi.ac.uk/pdbsum/1new PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1new ProSAT]</span></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=1new FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1new OCA], [https://pdbe.org/1new PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1new RCSB], [https://www.ebi.ac.uk/pdbsum/1new PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1new ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [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. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1new ConSurf]. | </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=1new ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The solution structure of Desulfuromonas acetoxidans cytochrome c7 has been refined by using 1H-NMR spectra recorded at 800 MHz and by using pseudocontact shifts in the final energy minimization procedure. The protein, composed of 68 amino acids, contains three paramagnetic heme moieties, each with one unpaired electron. The largely distributed paramagnetism broadens the lines in several protein parts. The structure is now relatively well resolved all over the backbone by the use of 1315 meaningful NOEs and 90 pseudocontact shifts. The statistical analysis of the structure indicates its satisfactory quality. The protein-fold is quite similar to that of the analogous four-heme cytochromes c3 for those parts which can be considered homologous. The solvent accessibility and the electrostatic potential surfaces surrounding the three hemes have been analyzed in terms of their reduction potentials. The resulting magnetic susceptibility anisotropy data obtained from pseudocontact shifts are analyzed in terms of structural data. | ||
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- | 800 MHz 1H NMR solution structure refinement of oxidized cytochrome c7 from Desulfuromonas acetoxidans.,Assfalg M, Banci L, Bertini I, Bruschi M, Turano P Eur J Biochem. 1998 Sep 1;256(2):261-70. PMID:9760163<ref>PMID:9760163</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1new" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | *[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Desulfuromonas acetoxidans]] | [[Category: Desulfuromonas acetoxidans]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Assfalg | + | [[Category: Assfalg M]] |
- | [[Category: Banci | + | [[Category: Banci L]] |
- | [[Category: Bertini | + | [[Category: Bertini I]] |
- | [[Category: Bruschi | + | [[Category: Bruschi M]] |
- | [[Category: Turano | + | [[Category: Turano P]] |
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Current revision
Cytochrome C551.5, NMR
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