1H, 13C and 15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli
Year: 2011
Type: article
Abstract: Viability and pathogenicity of Gram-negative bacteria is linked to the cytochrome c maturation and the oxidative protein folding systems in the periplasm. The transmembrane reductant conductor DsbD is a unique protein which provides the necessary reducing power to both systems through thiol-disulfide exchange reactions in a complex network of protein-protein interactions. The N-terminal domain of DsbD (nDsbD) is the delivery point of the reducing power originating from cytoplasmic thioredoxin to a variety of periplasmic partners. Here we report (1)H, (13)C and (15)N assignments for resonances of nDsbD in its oxidized and reduced states. These assignments provide the starting point for detailed investigations of the interactions of nDsbD with its protein partners.
Source: Biomolecular NMR Assignments
Institution: University of Oxford
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,890
Awards: Defining protein-protein interaction networks in cytochrome c assembly., Probing the activities of the Ccm proteins of the cytochrome c biosynthesis system, Bacterial transport and transformation of nitrate and nitrite in the nitrogen cycle, G6254867889, G8982310027, Nuclear magnetic resonance spectroscopy as a tool to study the structure, function, dynamics and folding of proteins: University Award for a research technologist in biomolecular NMR.
OpenAlex ID: W1989945668