This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4dhv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:35, 14 March 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==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]] 1.95&Aring;' scene=''>
+
<StructureSection load='4dhv' size='340' side='right'caption='[[4dhv]], [[Resolution|resolution]] 1.95&Aring;' 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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2z8q|2z8q]], [[3pni|3pni]], [[1sj1|1sj1]]</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='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'>[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'>[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;">
+
-
== 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 &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.
+
-
 
+
-
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>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 4dhv" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
*[[Ferredoxin|Ferredoxin]]
*[[Ferredoxin|Ferredoxin]]
-
*[[Journal:JBIC:19|Journal:JBIC:19]]
+
*[[Iron–sulfur proteins|Iron–sulfur proteins]]
-
== 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]]
+

Current revision

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

PDB ID 4dhv

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools