Fiche publication
Date publication
juillet 2009
Auteurs
Membres identifiés du Cancéropôle Est :
Pr BOSCHI-MULLER Sandrine
,
Dr JACOB Christophe
Tous les auteurs :
Quinternet M, Tsan P, Selme-Roussel L, Jacob C, Boschi-Muller S, Branlant G, Cung MT
Lien Pubmed
Résumé
DsbD transmembrane protein dispatches electrons to periplasmic Trx/DsbE-like partners via specific interactions with its N-terminal domain, nDsbD. In the present study, PilB N-terminal domain (NterPilB) is shown to efficiently accept electrons coming from nDsbD from Neisseria meningitidis. Using an NMR-driven docking approach, we have modeled the structure of a mixed disulfide complex between NterPilB and nDsbD. We show the needed opening of nDsbD cap-loop whereas NterPilB FLHE loop does not seem essential in the formation and stabilization of the complex. Relaxation analysis performed on backbone amide groups highlights a kind of dynamics transfer from nDsbD cap-loop on NterPilB alpha1 helix, suggesting that a mobility contribution is required not only for the formation of the mixed disulfide complex, but also for its disruption. Taking into account previous X-ray data on covalent complexes involving nDsbD, a cartoon of interactions between Trx-like partners and nDsbD is proposed that illustrates the adaptability of nDsbD.
Référence
Structure. 2009 Jul 15;17(7):1024-33.
