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==Ferredoxin VI from Rhodobacter Capsulatus== | |||
<StructureSection load='1e9m' size='340' side='right'caption='[[1e9m]], [[Resolution|resolution]] 2.07Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1e9m]] 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=1E9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E9M FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.07Å</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'>[https://proteopedia.org/fgij/fg.htm?mol=1e9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e9m OCA], [https://pdbe.org/1e9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e9m RCSB], [https://www.ebi.ac.uk/pdbsum/1e9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e9m ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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 == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e9/1e9m_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1e9m ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A [2Fe-2S] ferredoxin found in the photosynthetic bacterium Rhodobacter capsulatus has been purified in recombinant form from Escherichia coli. This protein, called FdVI, resembles ferredoxins involved in iron-sulfur cluster biosynthesis in various prokaryotic and eukaryotic cells. Purified recombinant FdVI was recovered in high yields and appeared to be indistinguishable from the genuine R. capsulatus ferredoxin based on UV-visible absorption and EPR spectroscopy and mass spectrometry. FdVI has been crystallized in the oxidized state by a sitting-drop vapour-diffusion technique using sodium formate as precipitant. Seeding larger drops from a previous hanging-drop-grown small crystal resulted in the formation of long red-brown prismatic needles. Preliminary X-ray diffraction analysis indicated that FdVI crystals are orthorhombic and belong to the space group P2(1)2(1)2(1), with unit-cell parameters a = 45.87, b = 49.83, c = 54.29 A. | |||
Crystallization and preliminary X-ray diffraction analysis of a [2Fe-2S] ferredoxin (FdVI) from Rhodobacter capsulatus.,Armengaud J, Sainz G, Jouanneau Y, Sieker LC Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):301-3. PMID:11173487<ref>PMID:11173487</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1e9m" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Ferredoxin|Ferredoxin]] | |||
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]] | |||
*[[IronâÂÂsulfur proteins|IronâÂÂsulfur proteins]] | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Rhodobacter capsulatus]] | [[Category: Rhodobacter capsulatus]] | ||
[[Category: Armengaud J]] | |||
[[Category: Armengaud | [[Category: Jouanneau Y]] | ||
[[Category: Jouanneau | [[Category: Larry S]] | ||
[[Category: Larry | [[Category: Sainz G]] | ||
[[Category: Sainz | [[Category: Sanishvili N]] | ||
[[Category: Sanishvili | [[Category: Stojanoff V]] | ||
[[Category: Stojanoff | |||
Latest revision as of 11:48, 9 May 2024
Ferredoxin VI from Rhodobacter CapsulatusFerredoxin VI from Rhodobacter Capsulatus
Structural highlights
FunctionFER6_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 PubMedA [2Fe-2S] ferredoxin found in the photosynthetic bacterium Rhodobacter capsulatus has been purified in recombinant form from Escherichia coli. This protein, called FdVI, resembles ferredoxins involved in iron-sulfur cluster biosynthesis in various prokaryotic and eukaryotic cells. Purified recombinant FdVI was recovered in high yields and appeared to be indistinguishable from the genuine R. capsulatus ferredoxin based on UV-visible absorption and EPR spectroscopy and mass spectrometry. FdVI has been crystallized in the oxidized state by a sitting-drop vapour-diffusion technique using sodium formate as precipitant. Seeding larger drops from a previous hanging-drop-grown small crystal resulted in the formation of long red-brown prismatic needles. Preliminary X-ray diffraction analysis indicated that FdVI crystals are orthorhombic and belong to the space group P2(1)2(1)2(1), with unit-cell parameters a = 45.87, b = 49.83, c = 54.29 A. Crystallization and preliminary X-ray diffraction analysis of a [2Fe-2S] ferredoxin (FdVI) from Rhodobacter capsulatus.,Armengaud J, Sainz G, Jouanneau Y, Sieker LC Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):301-3. PMID:11173487[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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