2fql

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(New page: 200px<br /><applet load="2fql" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fql, resolution 3.01&Aring;" /> '''Crystal structure of...)
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[[Image:2fql.gif|left|200px]]<br /><applet load="2fql" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2fql, resolution 3.01&Aring;" />
 
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'''Crystal structure of trimeric frataxin from the yeast Saccharomyces cerevisiae'''<br />
 
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==Overview==
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==Crystal structure of trimeric frataxin from the yeast Saccharomyces cerevisiae==
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Defects in the mitochondrial protein frataxin are responsible for, Friedreich ataxia, a neurodegenerative and cardiac disease that affects, 1:40,000 children. Here, we present the crystal structures of the, iron-free and iron-loaded frataxin trimers, and a single-particle electron, microscopy reconstruction of a 24 subunit oligomer. The structures reveal, fundamental aspects of the frataxin mechanism. The trimer has a central, channel in which one atom of iron binds. Two conformations of the channel, with different metal-binding affinities suggest that a gating mechanism, controls whether the bound iron is delivered to other proteins or, transferred to detoxification sites. The trimer constitutes the basic, structural unit of the 24 subunit oligomer. The architecture of this, oligomer and several features of the trimer structure demonstrate striking, similarities to the iron-storage protein ferritin. The data reveal how, stepwise assembly provides frataxin with the structural flexibility to, perform two functions: metal delivery and detoxification.
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<StructureSection load='2fql' size='340' side='right'caption='[[2fql]], [[Resolution|resolution]] 3.01&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2fql]] 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=2FQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FQL FirstGlance]. <br>
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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]] 3.01&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fql OCA], [https://pdbe.org/2fql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fql RCSB], [https://www.ebi.ac.uk/pdbsum/2fql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fql ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fq/2fql_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2fql ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Defects in the mitochondrial protein frataxin are responsible for Friedreich ataxia, a neurodegenerative and cardiac disease that affects 1:40,000 children. Here, we present the crystal structures of the iron-free and iron-loaded frataxin trimers, and a single-particle electron microscopy reconstruction of a 24 subunit oligomer. The structures reveal fundamental aspects of the frataxin mechanism. The trimer has a central channel in which one atom of iron binds. Two conformations of the channel with different metal-binding affinities suggest that a gating mechanism controls whether the bound iron is delivered to other proteins or transferred to detoxification sites. The trimer constitutes the basic structural unit of the 24 subunit oligomer. The architecture of this oligomer and several features of the trimer structure demonstrate striking similarities to the iron-storage protein ferritin. The data reveal how stepwise assembly provides frataxin with the structural flexibility to perform two functions: metal delivery and detoxification.
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==About this Structure==
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The structures of frataxin oligomers reveal the mechanism for the delivery and detoxification of iron.,Karlberg T, Schagerlof U, Gakh O, Park S, Ryde U, Lindahl M, Leath K, Garman E, Isaya G, Al-Karadaghi S Structure. 2006 Oct;14(10):1535-46. PMID:17027502<ref>PMID:17027502</ref>
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2FQL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FQL OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The structures of frataxin oligomers reveal the mechanism for the delivery and detoxification of iron., Karlberg T, Schagerlof U, Gakh O, Park S, Ryde U, Lindahl M, Leath K, Garman E, Isaya G, Al-Karadaghi S, Structure. 2006 Oct;14(10):1535-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17027502 17027502]
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</div>
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[[Category: Saccharomyces cerevisiae]]
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<div class="pdbe-citations 2fql" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Al-Karadaghi, S.]]
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[[Category: Karlberg, T.]]
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[[Category: alpha/beta sandwich]]
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[[Category: iron-storage]]
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[[Category: metallochaperone]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:42:30 2007''
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==See Also==
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*[[Frataxin|Frataxin]]
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*[[Frataxin 3D Structures|Frataxin 3D Structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Al-Karadaghi S]]
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[[Category: Karlberg T]]

Current revision

Crystal structure of trimeric frataxin from the yeast Saccharomyces cerevisiae

PDB ID 2fql

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