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==Crystal structure of trimeric frataxin from the yeast saccharomyces cerevisiae, complexed with cobalt==
==Crystal structure of trimeric frataxin from the yeast saccharomyces cerevisiae, complexed with cobalt==
<StructureSection load='3oer' size='340' side='right' caption='[[3oer]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='3oer' size='340' side='right'caption='[[3oer]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3oer]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OER OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OER FirstGlance]. <br>
<table><tr><td colspan='2'>[[3oer]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OER OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OER FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene><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]] 3.2&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fql|2fql]], [[3oeq|3oeq]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YFH1, YDL120W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</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=3oer FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oer OCA], [https://pdbe.org/3oer PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oer RCSB], [https://www.ebi.ac.uk/pdbsum/3oer PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oer ProSAT]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3oer FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oer OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oer RCSB], [http://www.ebi.ac.uk/pdbsum/3oer PDBsum]</span></td></tr>
</table>
<table>
== Function ==
[https://www.uniprot.org/uniprot/FRDA_YEAST FRDA_YEAST] Promotes the biosynthesis of heme as well as the assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. Plays a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+). Can store large amounts of the metal in the form of a ferrihydrite mineral by oligomerization. May be involved in regulation of the mitochondrial electron transport chain.<ref>PMID:9180083</ref> <ref>PMID:9988680</ref> <ref>PMID:15961414</ref> <ref>PMID:16371422</ref> <ref>PMID:19884169</ref> <ref>PMID:17027502</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Oligomerization Propensity and Flexibility of Yeast Frataxin Studied by X-ray Crystallography and Small-Angle X-ray Scattering.,Soderberg CA, Shkumatov AV, Rajan S, Gakh O, Svergun DI, Isaya G, Al-Karadaghi S J Mol Biol. 2011 Dec 16;414(5):783-97. Epub 2011 Oct 25. PMID:22051511<ref>PMID:22051511</ref>
Oligomerization Propensity and Flexibility of Yeast Frataxin Studied by X-ray Crystallography and Small-Angle X-ray Scattering.,Soderberg CA, Shkumatov AV, Rajan S, Gakh O, Svergun DI, Isaya G, Al-Karadaghi S J Mol Biol. 2011 Dec 16;414(5):783-97. Epub 2011 Oct 25. PMID:22051511<ref>PMID:22051511</ref>


From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3oer" style="background-color:#fffaf0;"></div>
==See Also==
*[[Frataxin 3D Structures|Frataxin 3D Structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Al-Karadaghi, S.]]
[[Category: Al-Karadaghi S]]
[[Category: Gakh, O.]]
[[Category: Gakh O]]
[[Category: Isaya, G.]]
[[Category: Isaya G]]
[[Category: Rajan, S.]]
[[Category: Rajan S]]
[[Category: Soderberg, C A.G.]]
[[Category: Soderberg CAG]]
[[Category: Ta, C.]]
[[Category: Ta C]]
[[Category: Alpha/beta sandwich]]
[[Category: Iron-storage]]
[[Category: Metallochaperone]]
[[Category: Transport protein]]
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