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| | ==reduced ferredoxin 6 from Rhodobacter capsulatus== | | ==reduced ferredoxin 6 from Rhodobacter capsulatus== |
| - | <StructureSection load='1uwm' size='340' side='right' caption='[[1uwm]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='1uwm' size='340' side='right'caption='[[1uwm]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1uwm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"rhodonostoc_capsulatum"_molisch_1907 "rhodonostoc capsulatum" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UWM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UWM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1uwm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UWM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UWM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e9m|1e9m]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=1uwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uwm OCA], [http://pdbe.org/1uwm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uwm RCSB], [http://www.ebi.ac.uk/pdbsum/1uwm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1uwm 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=1uwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uwm OCA], [https://pdbe.org/1uwm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uwm RCSB], [https://www.ebi.ac.uk/pdbsum/1uwm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uwm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FER6_RHOCA FER6_RHOCA]] Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | + | [https://www.uniprot.org/uniprot/FER6_RHOCA FER6_RHOCA] Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Ferredoxin|Ferredoxin]] | + | *[[Ferredoxin 3D structures|Ferredoxin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Rhodonostoc capsulatum molisch 1907]] | + | [[Category: Large Structures]] |
| - | [[Category: Armengaud, J]] | + | [[Category: Rhodobacter capsulatus]] |
| - | [[Category: Asso, M]] | + | [[Category: Armengaud J]] |
| - | [[Category: Bertrand, P]] | + | [[Category: Asso M]] |
| - | [[Category: Jakoncic, J]] | + | [[Category: Bertrand P]] |
| - | [[Category: Jouanneau, Y]] | + | [[Category: Jakoncic J]] |
| - | [[Category: Sainz, G]] | + | [[Category: Jouanneau Y]] |
| - | [[Category: Sanishvili, N]] | + | [[Category: Sainz G]] |
| - | [[Category: Sieker, L C]] | + | [[Category: Sanishvili N]] |
| - | [[Category: Stojanoff, V]] | + | [[Category: Sieker LC]] |
| - | [[Category: 2fe-2]]
| + | [[Category: Stojanoff V]] |
| - | [[Category: Electron transport]]
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| - | [[Category: Ferredoxin]]
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| - | [[Category: Iron]]
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| - | [[Category: Iron-sulfur]]
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| - | [[Category: Metal-binding]]
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| Structural highlights
Function
FER6_RHOCA Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
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
FdVI from Rhodobacter capsulatus is structurally related to a group of [2Fe-2S] ferredoxins involved in iron-sulfur cluster biosynthesis. Comparative genomics suggested that FdVI and orthologs found in alpha-Proteobacteria are involved in this process. Here, the crystal structure of FdVI has been determined for both the oxidized and the reduced protein. The [2Fe-2S] cluster lies 6 A below the protein surface in a hydrophobic pocket without access to the solvent. This particular cluster environment might explain why the FdVI midpoint redox potential (-306 mV at pH 8.0) did not show temperature or ionic strength dependence. Besides the four cysteines that bind the cluster, FdVI features an extra cysteine which is located close to the S1 atom of the cluster and is oriented in a position such that its thiol group points towards the solvent. Upon reduction, the general fold of the polypeptide chain was almost unchanged. The [2Fe-2S] cluster underwent a conformational change from a planar to a distorted lozenge. In the vicinity of the cluster, the side chain of Met24 was rotated by 180 degrees , bringing its S atom within hydrogen-bonding distance of the S2 atom of the cluster. The reduced molecule also featured a higher content of bound water molecules, and more extensive hydrogen-bonding networks compared with the oxidized molecule. The unique conformational changes observed in FdVI upon reduction are discussed in the light of structural studies performed on related ferredoxins.
Structure of a [2Fe-2S] ferredoxin from Rhodobacter capsulatus likely involved in Fe-S cluster biogenesis and conformational changes observed upon reduction.,Sainz G, Jakoncic J, Sieker LC, Stojanoff V, Sanishvili N, Asso M, Bertrand P, Armengaud J, Jouanneau Y J Biol Inorg Chem. 2006 Mar;11(2):235-46. Epub 2006 Jan 10. PMID:16402206[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sainz G, Jakoncic J, Sieker LC, Stojanoff V, Sanishvili N, Asso M, Bertrand P, Armengaud J, Jouanneau Y. Structure of a [2Fe-2S] ferredoxin from Rhodobacter capsulatus likely involved in Fe-S cluster biogenesis and conformational changes observed upon reduction. J Biol Inorg Chem. 2006 Mar;11(2):235-46. Epub 2006 Jan 10. PMID:16402206 doi:10.1007/s00775-005-0069-2
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