Analyse structurale et dynamique par RMN des domaines N-terminaux des protéines DsbD et PilB de Neisseria meningitidis et de leur interaction

Abstract : We show, on one hand, that the NMR solution structure of DsbD N-terminal domain from Neisseria meningitidis (nDsbD) displays, in its reduced state, an immunoglobulin fold with a closed conformation of its active site. Nonetheless, our backbone dynamics study shows that the cap-loop region of the protein, which covers active residues in both oxidized and reduced forms, displays internal motions. This illustrates the inner structural adjustment capacities of nDsbD. On the other hand, we show that NMR solution structures of the oxidized and reduced forms of N. meningitidis NterPilB display a thioredoxin-like fold. These two structures appear to be very similar and globally rigid. Consequently, the NterPilB characteristic FLHE loop, which covers one edge of the active site, does not reveal new structural and/or dynamics properties for its involvement in the substrate specificity. Finally, we point out, from the structural and dynamics study of a complex between nDsbD and NterPilB from N. meningitidis, that nDsbD exhibits a powerful adaptability in its complex state. Its cap-loop region opens and comes over the a helix containing the NterPilB active cysteines. In contrast, the NterPilB FLHE loop does not seem to play a role in the complex stabilization. We propose that internal dynamics should facilitate, on one hand, the relative adaptability between the two partners of the complex and, on the other hand, their subsequent dissociation
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Marc Quinternet. Analyse structurale et dynamique par RMN des domaines N-terminaux des protéines DsbD et PilB de Neisseria meningitidis et de leur interaction. Sciences agricoles. Institut National Polytechnique de Lorraine, 2008. Français. ⟨NNT : 2008INPL102N⟩. ⟨tel-01753012⟩

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