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Analyse structurale par RMN des interactions de la MsrB de Neisseria meningitidis avec ses partenaires biologiques :

Abstract : Methionine sulfoxides (MetSO) are easily formed in proteins exposed to reactive oxidative species commonly present in cells. Structural modification and modulation of their activity are the consequence of the oxidation of the protein methionines. Their reduction, back to methionines, is catalyzed by methionine sulfoxide reductases (Msr). These enzymes play a beneficial role in aging process but are involve in the virulence of some bacteria. Msr's are divided in two classes, named MsrA and MsrB, which display opposite stereoselectivities toward the sulfoxide center site. In this PhD thesis, we present studies of the conformational changes of the Neisseria meningitidis MsrB by NMR with the purpose of characterising the catalytic mechanism of the MsrB and of understanding the interaction between MsrB and its partners (MetSO and thioredoxin). From the 1H, 13C and 15N resonance assignments of the reduced from of MsrB, we conclude that the predicted secondary structures are in agreement with those obtained from the X-ray data of the Neisseria gonorrhoeae MsrB. Interaction studies of MsrB with a sulfoxyde substrat show that the active site is not the only one perturbed by the binding. The two next intermediates which are formed along the reaction are a MsrB which possesses a sulfenic acid and a MsrB with a locally specific disulfide bridge. Studies of these two intermediates reveal a structural change during the protein oxidation. Specific interaction between Trx and the oxidized MsrB leads to the reduction of the latter which recovers its starting 3D structure
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Aurélien Thureau. Analyse structurale par RMN des interactions de la MsrB de Neisseria meningitidis avec ses partenaires biologiques :. Autre. Institut National Polytechnique de Lorraine, 2005. Français. ⟨NNT : 2005INPL072N⟩. ⟨tel-01752517⟩

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