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-Structure paper
タイトル | Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. |
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ジャーナル・号・ページ | Nat Commun, Vol. 1, Issue 7, Page 95, Year 2010 |
掲載日 | 2010年10月19日 |
著者 | Filippo Prischi / Petr V Konarev / Clara Iannuzzi / Chiara Pastore / Salvatore Adinolfi / Stephen R Martin / Dmitri I Svergun / Annalisa Pastore / |
PubMed 要旨 | Reduced levels of frataxin, an essential protein of as yet unknown function, are responsible for causing the neurodegenerative pathology Friedreich's ataxia. Independent reports have linked frataxin ...Reduced levels of frataxin, an essential protein of as yet unknown function, are responsible for causing the neurodegenerative pathology Friedreich's ataxia. Independent reports have linked frataxin to iron-sulphur cluster assembly through interactions with the two central components of this machinery: desulphurase Nfs1/IscS and the scaffold protein Isu/IscU. In this study, we use a combination of biophysical methods to define the structural bases of the interaction of CyaY (the bacterial orthologue of frataxin) with the IscS/IscU complex. We show that CyaY binds IscS as a monomer in a pocket between the active site and the IscS dimer interface. Recognition does not require iron and occurs through electrostatic interactions of complementary charged residues. Mutations at the complex interface affect the rates of enzymatic cluster formation. CyaY binding strengthens the affinity of the IscS/IscU complex. Our data suggest a new paradigm for understanding the role of frataxin as a regulator of IscS functions. |
リンク | Nat Commun / PubMed:20981023 / PubMed Central |
手法 | SAS (X-ray synchrotron) |
構造データ | SASDA27: SASDAV6: SASDAW6: SASDAX6: SASDAY6: SASDAZ6: |
由来 |
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