2fql
From Proteopedia
(New page: 200px<br /><applet load="2fql" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fql, resolution 3.01Å" /> '''Crystal structure of...) |
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| - | [[Image:2fql.gif|left|200px]]<br /><applet load="2fql" size=" | + | [[Image:2fql.gif|left|200px]]<br /><applet load="2fql" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fql, resolution 3.01Å" /> | caption="2fql, resolution 3.01Å" /> | ||
'''Crystal structure of trimeric frataxin from the yeast Saccharomyces cerevisiae'''<br /> | '''Crystal structure of trimeric frataxin from the yeast Saccharomyces cerevisiae'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Defects in the mitochondrial protein frataxin are responsible for | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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://oca.weizmann.ac.il/oca-bin/ocashort?id=2FQL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: metallochaperone]] | [[Category: metallochaperone]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:24:08 2008'' |
Revision as of 15:24, 21 February 2008
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Crystal structure of trimeric frataxin from the yeast Saccharomyces cerevisiae
Overview
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.
About this Structure
2FQL is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
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
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