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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 1H, 13C and 15N 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. © 2011 The Author(s).

Original publication




Journal article


Biomolecular NMR Assignments

Publication Date



1 - 5


Escherichia coli DsbD, NMR resonance assignments, Oxidation/reduction, Oxidoreductase, Thiol:disulfide exchange reaction