2FQL

Crystal structure of trimeric frataxin from the yeast Saccharomyces cerevisiae

Summary for 2FQL

• Entry DOI: 10.2210/pdb2fql/pdb
• Descriptor: Frataxin homolog, mitochondrial (1 entity in total)
• Functional Keywords: alpha/beta sandwich, metallochaperone, iron-storage, transport protein
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Mitochondrion matrix : Q07540
• Total number of polymer chains: 1
• Total formula weight: 13671.18

Authors

Al-Karadaghi, S.,Karlberg, T. (deposition date: 2006-01-18, release date: 2006-11-07, Last modification date: 2023-08-30)

Primary citation

Karlberg, T.,Schagerlof, U.,Gakh, O.,Park, S.,Ryde, U.,Lindahl, M.,Leath, K.,Garman, E.,Isaya, G.,Al-Karadaghi, S.
The structures of frataxin oligomers reveal the mechanism for the delivery and detoxification of iron.
Structure, 14:1535-1546, 2006

PubMed Abstract: 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.

PubMed: 17027502
DOI: 10.1016/j.str.2006.08.010

Experimental method

X-RAY DIFFRACTION (3.01 Å)