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Bacterial growth and pathogenicity depend on the correct formation of disulfide bonds, a process controlled by the Dsb system in the periplasm of Gram-negative bacteria. Proteins with a thioredoxin fold play a central role in this process. A general feature of thiol-disulfide exchange reactions is the need to avoid a long lived product complex between protein partners. We use a multidisciplinary approach, involving NMR, x-ray crystallography, surface plasmon resonance, mutagenesis, and in vivo experiments, to investigate the interaction between the two soluble domains of the transmembrane reductant conductor DsbD. Our results show oxidation state-dependent affinities between these two domains. These observations have implications for the interactions of the ubiquitous thioredoxin-like proteins with their substrates, provide insight into the key role played by a unique redox partner with an immunoglobulin fold, and are of general importance for oxidative protein-folding pathways in all organisms.

Original publication




Journal article


J Biol Chem

Publication Date





24943 - 24956


Crystallography, X-Ray, Disulfides, Escherichia coli, Escherichia coli Proteins, Magnetic Resonance Spectroscopy, Mutagenesis, Oxidation-Reduction, Oxidoreductases, Protein Folding, Protein Structure, Tertiary, Surface Plasmon Resonance