Titre | Solution structure and backbone dynamics of the cysteine 103 to serine mutant of the N-terminal domain of DsbD from Neisseria meningitidis. |
Publication Type | Journal Article |
Year of Publication | 2008 |
Authors | Quinternet, M, Tsan, P, Selme, L, Beaufils, C, Jacob, C, Boschi-Muller, S, Averlant-Petit, M-C, Branlant, G, Cung, M-T |
Journal | Biochemistry |
Volume | 47 |
Issue | 48 |
Pagination | 12710-20 |
Date Published | 2008 Dec 2 |
ISSN | 1520-4995 |
Mots-clés | Catalytic Domain, Cysteine, Magnetic Resonance Spectroscopy, Models, Molecular, Mutant Proteins, Mutation, Neisseria meningitidis, Oxidoreductases, Protein Structure, Tertiary, Serine, Solutions |
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. |
DOI | 10.1021/bi801343c |
Alternate Journal | Biochemistry |
PubMed ID | 18983169 |