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4dhv

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Current revision (14:35, 14 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<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>
<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>
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</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>
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</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>
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<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='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='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>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/FER_PYRFU FER_PYRFU]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
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[https://www.uniprot.org/uniprot/FER_PYRFU FER_PYRFU] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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 &lt;/= D14C &lt; D14H and shows the same trend as reported for the variants containing the [Fe(3)S(4)] cluster, but is different from the D14C &lt; D14H &lt; 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.
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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<ref>PMID:23296387</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4dhv" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Ferredoxin|Ferredoxin]]
*[[Ferredoxin|Ferredoxin]]
*[[Iron–sulfur proteins|Iron–sulfur proteins]]
*[[Iron–sulfur proteins|Iron–sulfur proteins]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Crystal structure of the Pyrococcus furiosus ferredoxin D14C variant containing the heterometallic [AgFe3S4] cluster

PDB ID 4dhv

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