2k0r

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

spinqualitylabelsall models 2k0r, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2k0r is a 1 chain structure with sequence from Neisseria meningitidis serogroup b. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: dsbD, NMB1519 (Neisseria meningitidis serogroup B) Activity: Protein-disulfide reductase, with EC number 1.8.1.8 Resources: FirstGlance, OCA, RCSB, PDBsum Function [DSBD_NEIMB] Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Solution Structure and Backbone Dynamics of the Cysteine 103 to Serine Mutant of the N-Terminal Domain of DsbD from Neisseria meningitides.,Quinternet M, Tsan P, Selme L, Beaufils C, Jacob C, Boschi-Muller S, Averlant-Petit MC, Branlant G, Cung MT Biochemistry. 2008 Nov 5. PMID:18983169 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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