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Détermination de la structure par RMN d'une protéine impliquée dans la biosynthèse de centres [Fe-S]: SufA

Abstract : The SufA protein from Escherichia coli is a homodimeric scaffold protein, allowing the formation of iron-sulfur clusters [Fe-S] before forwarding them to a target protein. This protein belongs to the SUF (for sulfur mobilzation) operon which appears to be activited under oxidative stress. In order to have a better understanding of the coordination of the [Fe-S] by the SufA protein, we undertook the determination of the three-dimensional structure by nuclear magnetic resonance (NMR). Currently, we achieved on the monomeric form of the apo-protein. Preliminary results with the reconstituted [Fe-S] protein are also presented in this document. We were able to observe the presence of three cysteine residues whose role, which was determinated by biochemical studies, is to stabilize the [Fe-S] cluster. However the exact coordination of the [Fe-S] cluster by these cysteines is not well known. The structure resolution of the dimer (in progress), and complementary NMR studies on the holoprotein SufA should bring a better understanding of the coordination mode of its cluster. It is worth to note that structural differences, with regard to the X-ray structures (published during this thesis) were observed, located particulary in the C-terminal sequence who we find two over the three coordinating cysteines.
Mots-clés : RMN
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https://tel.archives-ouvertes.fr/tel-00200198
Contributor : Nicolas Duraffourg <>
Submitted on : Thursday, December 20, 2007 - 3:20:25 PM
Last modification on : Wednesday, November 4, 2020 - 1:46:51 PM
Long-term archiving on: : Thursday, September 27, 2012 - 12:05:37 PM

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Nicolas Duraffourg. Détermination de la structure par RMN d'une protéine impliquée dans la biosynthèse de centres [Fe-S]: SufA. Biophysique [physics.bio-ph]. Université Joseph-Fourier - Grenoble I, 2006. Français. ⟨tel-00200198⟩

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