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1new

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Revision as of 23:49, 11 September 2015

Cytochrome C551.5, NMR

Structural highlights

1new is a 1 chain structure with sequence from Desulfuromonas acetoxidans. This structure supersedes the now removed PDB entries 2new and 1cfo. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[CYC3_DESAC] Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Assfalg M, Banci L, Bertini I, Bruschi M, Turano P. 800 MHz 1H NMR solution structure refinement of oxidized cytochrome c7 from Desulfuromonas acetoxidans. Eur J Biochem. 1998 Sep 1;256(2):261-70. PMID:9760163

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1new"

@@ Line 2: / Line 2: @@
 <StructureSection load='1new' size='340' side='right' caption='[[1new]], [[NMR_Ensembles_of_Models | 35 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1new]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Desulfuromonas_acetoxidans Desulfuromonas acetoxidans]. This structure supersedes the now removed PDB entries  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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NEW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1new]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NEW FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1new FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1new OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1new RCSB], [http://www.ebi.ac.uk/pdbsum/1new PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1new FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1new OCA], [http://pdbe.org/1new PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1new RCSB], [http://www.ebi.ac.uk/pdbsum/1new PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1new" style="background-color:#fffaf0;"></div>
 ==See Also==

1new

From Proteopedia

Revision as of 23:49, 11 September 2015

Cytochrome C551.5, NMR

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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