Oxidation state-dependent protein-protein interactions in disulfide cascades

Despoina A I Mavridou, Paraskevi Kritsiligkou, Emmanuel Saridakis, Alan D Goddard, Julie M Stevens, Stuart J Ferguson, Christina Redfield

    Research output: Contribution to journalArticlepeer-review


    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 languageEnglish
    Pages (from-to)24943-56
    Number of pages14
    JournalJournal of Biological Chemistry
    Issue number28
    Publication statusPublished - 15 Jul 2011


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


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