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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.

Original publication




Journal article


Biomol NMR Assign

Publication Date





163 - 167


Carbon Isotopes, Escherichia coli, Escherichia coli Proteins, Nitrogen Isotopes, Nuclear Magnetic Resonance, Biomolecular, Oxidation-Reduction, Oxidoreductases, Protein Structure, Tertiary, Protons