1ekg: Difference between revisions

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[[Image:1ekg.jpg|left|200px]]
{{Seed}}
[[Image:1ekg.png|left|200px]]


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{{STRUCTURE_1ekg|  PDB=1ekg  |  SCENE=  }}  
{{STRUCTURE_1ekg|  PDB=1ekg  |  SCENE=  }}  


'''MATURE HUMAN FRATAXIN'''
===MATURE HUMAN FRATAXIN===




==Overview==
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Friedreich's ataxia, an autosomal recessive neurodegenerative disorder characterized by progressive gait and limb ataxia, cardiomyopathy, and diabetes mellitus, is caused by decreased frataxin production or function. The structure of human frataxin, which we have determined at 1.8-A resolution, reveals a novel protein fold. A five-stranded, antiparallel beta sheet provides a flat platform, which supports a pair of parallel alpha helices, to form a compact alphabeta sandwich. A cluster of 12 acidic residues from the first helix and the first strand of the large sheet form a contiguous anionic surface on the protein. The overall protein structure and the anionic patch are conserved in eukaryotes, including animals, plants, and yeast, and in prokaryotes. Additional conserved residues create an extended 1008-A(2) patch on a distinct surface of the protein. Side chains of disease-associated mutations either contribute to the anionic patch, help create the second conserved surface, or point toward frataxin's hydrophobic core. These structural findings predict potential modes of protein-protein and protein-iron binding.
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{{ABSTRACT_PUBMED_10900192}}


==About this Structure==
==About this Structure==
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[[Category: Iron transport]]
[[Category: Iron transport]]
[[Category: Mitochondrial]]
[[Category: Mitochondrial]]
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Revision as of 21:53, 30 June 2008

File:1ekg.png

Template:STRUCTURE 1ekg

MATURE HUMAN FRATAXIN

Template:ABSTRACT PUBMED 10900192

About this Structure

1EKG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human frataxin., Dhe-Paganon S, Shigeta R, Chi YI, Ristow M, Shoelson SE, J Biol Chem. 2000 Oct 6;275(40):30753-6. PMID:10900192

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