2K9F
Structural features of the complex between the DsbD N-terminal and the PilB N-terminal domains from Neisseria meningitidis
Summary for 2K9F
| Entry DOI | 10.2210/pdb2k9f/pdb |
| Related | 2jzs 2k0r |
| Descriptor | Thioredoxin, Thiol:disulfide interchange protein dsbD (2 entities in total) |
| Functional Keywords | protein, docking, thioredoxin, immunoglobulin, dsbd, pilb, electron transport, multifunctional enzyme, oxidoreductase, redox-active center, transport, cytochrome c-type biogenesis, inner membrane, membrane, nad, transmembrane |
| Biological source | Neisseria meningitidis serogroup A More |
| Cellular location | Cell inner membrane; Multi-pass membrane protein (By similarity): Q9JYM0 |
| Total number of polymer chains | 2 |
| Total formula weight | 30016.83 |
| Authors | Quinternet, M.,Tsan, P.,Selme, L.,Jacob, C.,Boschi-Muller, S.,Branlant, G.,Cung, M. (deposition date: 2008-10-09, release date: 2009-05-19, Last modification date: 2024-10-16) |
| Primary citation | Quinternet, M.,Tsan, P.,Selme-Roussel, L.,Jacob, C.,Boschi-Muller, S.,Branlant, G.,Cung, M.T. Formation of the complex between DsbD and PilB N-terminal domains from Neisseria meningitidis necessitates an adaptability of nDsbD. Structure, 17:1024-1033, 2009 Cited by PubMed 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. PubMed: 19604482DOI: 10.1016/j.str.2009.05.011 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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