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| | ==Crystal structure of the Pyrococcus furiosus ferredoxin D14C variant containing the heterometallic [AgFe3S4] cluster== | | ==Crystal structure of the Pyrococcus furiosus ferredoxin D14C variant containing the heterometallic [AgFe3S4] cluster== |
| - | <StructureSection load='4dhv' size='340' side='right' caption='[[4dhv]], [[Resolution|resolution]] 1.95Å' scene=''> | + | <StructureSection load='4dhv' size='340' side='right'caption='[[4dhv]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4dhv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrfu Pyrfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DHV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DHV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4dhv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_DSM_3638 Pyrococcus furiosus DSM 3638]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DHV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0KA:SILVER/IRON/SULFUR+CLUSTER'>0KA</scene>, <scene name='pdbligand=NCO:COBALT+HEXAMMINE(III)'>NCO</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0KA:SILVER/IRON/SULFUR+CLUSTER'>0KA</scene>, <scene name='pdbligand=NCO:COBALT+HEXAMMINE(III)'>NCO</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2z8q|2z8q]], [[3pni|3pni]], [[1sj1|1sj1]]</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=4dhv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dhv OCA], [https://pdbe.org/4dhv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dhv RCSB], [https://www.ebi.ac.uk/pdbsum/4dhv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dhv ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fdxA, Ferredoxin, PF1909 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</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=4dhv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dhv OCA], [http://pdbe.org/4dhv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dhv RCSB], [http://www.ebi.ac.uk/pdbsum/4dhv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dhv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FER_PYRFU FER_PYRFU]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | + | [[https://www.uniprot.org/uniprot/FER_PYRFU FER_PYRFU]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| | *[[Ferredoxin|Ferredoxin]] | | *[[Ferredoxin|Ferredoxin]] |
| - | *[[Journal:JBIC:19|Journal:JBIC:19]] | + | *[[IronâÂÂsulfur proteins|IronâÂÂsulfur proteins]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Pyrfu]] | + | [[Category: Large Structures]] |
| - | [[Category: Christensen, H E.M]] | + | [[Category: Pyrococcus furiosus DSM 3638]] |
| - | [[Category: Haahr, L T]] | + | [[Category: Christensen HEM]] |
| - | [[Category: Jakab-Simon, I N]] | + | [[Category: Haahr LT]] |
| - | [[Category: Artificial metalloprotein]] | + | [[Category: Jakab-Simon IN]] |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Ferredoxin]]
| + | |
| - | [[Category: Heterometallic]]
| + | |
| - | [[Category: Iron-sulfur protein]]
| + | |
| - | [[Category: Pyrococcus furiosus]]
| + | |
| - | [[Category: Silver]]
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| Structural highlights
Function
[FER_PYRFU] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Publication Abstract from PubMed
Heterometallic [AgFe(3)S(4)] iron-sulfur clusters assembled in wild-type Pyrococcus furiosus ferredoxin and two variants, D14C and D14H, are characterized. The crystal structure of the [AgFe(3)S(4)] D14C variant shows that the silver(I) ion is indeed part of the cluster and is coordinated to the thiolate group of residue 14. Cyclic voltammetry shows one redox pair with a reduction potential of +220 mV versus the standard hydrogen electrode which is assigned to the [AgFe(3)S(4)](2+/+) couple. The oxidized form of the [AgFe(3)S(4)] D14C variant is stable in the presence of dioxygen, whereas the oxidized forms of the [AgFe(3)S(4)] wild type and D14H variants convert to the [Fe(3)S(4)] ferredoxin form. The monovalent d (10) silver(I) ion stabilizes the [Fe(3)S(4)](+/0) cluster fragment, as opposed to divalent d (10) metal ions, resulting in more than 0.4 V difference in reduction potentials between the silver(I) and, e.g., zinc(II) heterometallic [MFe(3)S(4)] ferredoxins. The trend in reduction potentials for the variants containing the [AgFe(3)S(4)] cluster is wild type </= D14C < D14H and shows the same trend as reported for the variants containing the [Fe(3)S(4)] cluster, but is different from the D14C < D14H < wild type trend reported for the [Fe(4)S(4)] ferredoxin. The similarity in the reduction potential trend for the variants containing the heterometallic [AgFe(3)S(4)] cluster and the [Fe(3)S(4)] cluster can be rationalized in terms of the electrostatic influence of the residue 14 side chains, rather than the dissociation constant of this residue, as is the case for [Fe(4)S(4)] ferredoxins. The trends in reduction potentials are in line with there being no electronic coupling between the silver(I) ion and the Fe(3)S(4) fragment.
Heterometallic [AgFe(3)S (4)] ferredoxin variants: synthesis, characterization, and the first crystal structure of an engineered heterometallic iron-sulfur protein.,Martic M, Jakab-Simon IN, Haahr LT, Hagen WR, Christensen HE J Biol Inorg Chem. 2013 Feb;18(2):261-76. doi: 10.1007/s00775-012-0971-3. Epub, 2013 Jan 8. PMID:23296387[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Martic M, Jakab-Simon IN, Haahr LT, Hagen WR, Christensen HE. Heterometallic [AgFe(3)S (4)] ferredoxin variants: synthesis, characterization, and the first crystal structure of an engineered heterometallic iron-sulfur protein. J Biol Inorg Chem. 2013 Feb;18(2):261-76. doi: 10.1007/s00775-012-0971-3. Epub, 2013 Jan 8. PMID:23296387 doi:10.1007/s00775-012-0971-3
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