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1ly7

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{{STRUCTURE_1ly7| PDB=1ly7 | SCENE= }}
{{STRUCTURE_1ly7| PDB=1ly7 | SCENE= }}
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'''The solution structure of the the c-terminal domain of frataxin, the protein responsible for friedreich ataxia'''
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===The solution structure of the the c-terminal domain of frataxin, the protein responsible for friedreich ataxia===
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==Overview==
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BACKGROUND: Lesions in the gene for frataxin, a nuclear-encoded mitochondrial protein, cause the recessively inherited condition Friedreich's ataxia. It is thought that the condition arises from disregulation of mitochondrial iron homeostasis, with concomitant oxidative damage leading to neuronal death. Very little is, as yet, known about the biochemical function of frataxin. RESULTS: Here, we show that the mature form of recombinant frataxin behaves in solution as a monodisperse species that is composed of a 15-residue-long unstructured N terminus and an evolutionarily conserved C-terminal region that is able to fold independently. The structure of the C-terminal domain consists of a stable seven-stranded antiparallel beta sheet packing against a pair of parallel helices. The structure is compact with neither grooves nor cavities, features that are typical of iron-binding modules. Exposed evolutionarily conserved residues cover a broad area and all cluster on the beta-sheet face of the structure, suggesting that this is a functionally important surface. The effect of two clinically occurring mutations on the fold was checked experimentally. When the mature protein was titrated with iron, no tendency to iron-binding or to aggregation was observed. CONCLUSIONS: Knowledge of the frataxin structure provides important guidelines as to the nature of the frataxin binding partner. The absence of all the features expected for an iron-binding activity, the large conserved area on its surface and lack of evidence for iron-binding activity strongly support an indirect involvement of frataxin in iron metabolism. The effects of point mutations associated with Friedreich's ataxia can be rationalised by knowledge of the structure and suggest possible models for the occurrence of the disease in compound heterozygous patients.
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(as it appears on PubMed at http://www.pubmed.gov), where 10903947 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10903947}}
==About this Structure==
==About this Structure==
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1LY7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1dlx 1dlx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LY7 OCA].
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1LY7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1dlx 1dlx]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LY7 OCA].
==Reference==
==Reference==
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[[Category: Stier, G.]]
[[Category: Stier, G.]]
[[Category: Alpha-beta]]
[[Category: Alpha-beta]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:24:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:48:02 2008''

Revision as of 19:48, 2 July 2008

Image:1ly7.png

Template:STRUCTURE 1ly7

The solution structure of the the c-terminal domain of frataxin, the protein responsible for friedreich ataxia

Template:ABSTRACT PUBMED 10903947

About this Structure

1LY7 is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1dlx. Full experimental information is available from OCA.

Reference

Towards a structural understanding of Friedreich's ataxia: the solution structure of frataxin., Musco G, Stier G, Kolmerer B, Adinolfi S, Martin S, Frenkiel T, Gibson T, Pastore A, Structure. 2000 Jul 15;8(7):695-707. PMID:10903947

Page seeded by OCA on Wed Jul 2 22:48:02 2008

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