title: Formation of the complex between DsbD and PilB N-terminal domains from Neisseria meningitidis necessitates an adaptability of nDsbD.
abstract: 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.
authors: Laboratoire de Chimie Physique Macromoléculaire UMR 7568 CNRS-INPL, Nancy Université, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France.
authors: Marc
authors: M
authors: Quinternet
authors: Pascale
authors: P
authors: Tsan
authors: Laure
authors: L
authors: Selme-Roussel
authors: Christophe
authors: C
authors: Jacob
authors: Sandrine
authors: S
authors: Boschi-Muller
authors: Guy
authors: G
authors: Branlant
authors: Manh-Thong
authors: MT
authors: Cung
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D001665:Binding Sites; D004220:Disulfides / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D004583:Electrons; D007700:Kinetics; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D009345:Neisseria meningitidis / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular; D010088:Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D019897:Periplasm / Q000378:metabolism; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D001426:Bacterial Proteins; D004220:Disulfides; D008565:Membrane Proteins; D010088:Oxidoreductases; C068255:pilB protein, Bacteria