2K0R

Solution structure of the C103S mutant of the N-terminal Domain of DsbD from Neisseria meningitidis

Summary for 2K0R

• Entry DOI: 10.2210/pdb2k0r/pdb
• Descriptor: Thiol:disulfide interchange protein dsbD (1 entity in total)
• Functional Keywords: immunoglobulin, mutant, n-terminal domain, disulfide bond reductase, cytochrome c-type biogenesis, electron transport, inner membrane, membrane, nad, oxidoreductase, redox-active center, transmembrane, transport
• Biological source: Neisseria meningitidis serogroup B
• Cellular location: Cell inner membrane; Multi-pass membrane protein (By similarity): Q9JYM0
• Total number of polymer chains: 1
• Total formula weight: 14168.74

Authors

Quinternet, M.,Selme, L.,Tsan, P.,Beaufils, C.,Jacob, C.,Boschi-Muller, S.,Averlant-Petit, M.,Branlant, G.,Cung, M. (deposition date: 2008-02-13, release date: 2008-11-11, Last modification date: 2024-05-29)

Primary citation

Quinternet, M.,Tsan, P.,Selme, L.,Beaufils, C.,Jacob, C.,Boschi-Muller, S.,Averlant-Petit, M.C.,Branlant, G.,Cung, M.T.
Solution structure and backbone dynamics of the cysteine 103 to serine mutant of the N-terminal domain of DsbD from Neisseria meningitidis.
Biochemistry, 47:12710-12720, 2008

PubMed Abstract: The DsbD protein is essential for electron transfer from the cytoplasm to the periplasm of Gram-negative bacteria. Its N-terminal domain dispatches electrons coming from cytoplasmic thioredoxin (Trx), via its central transmembrane and C-terminal domains, to its periplasmic partners: DsbC, DsbE/CcmG, and DsbG. Previous structural studies described the latter proteins as Trx-like folds possessing a characteristic C-X-X-C motif able to generate a disulfide bond upon oxidation. The Escherichia coli nDsbD displays an immunoglobulin-like fold in which two cysteine residues (Cys103 and Cys109) allow a disulfide bond exchange with its biological partners.We have determined the structure in solution and the backbone dynamics of the C103S mutant of the N-terminal domain of DsbD from Neisseria meningitidis. Our results highlight significant structural changes concerning the beta-sheets and the local topology of the active site compared with the oxidized form of the E. coli nDsbD. The structure reveals a "cap loop" covering the active site, similar to the oxidized E. coli nDsbD X-ray structure. However, regions featuring enhanced mobility were observed both near to and distant from the active site, revealing a capacity of structural adjustments in the active site and in putative interaction areas with nDsbD biological partners. Results are discussed in terms of functional consequences.

PubMed: 18983169
DOI: 10.1021/bi801343c

Experimental method

SOLUTION NMR