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Proteins belonging to the thioredoxin (Trx) superfamily are abundant in all organisms. They share the same structural features, arranged in a seemingly simple fold, but they perform a multitude of functions in oxidative protein folding and electron transfer pathways. We use the C-terminal domain of the unique transmembrane reductant conductor DsbD as a model for an in-depth analysis of the factors controlling the reactivity of the Trx fold. We employ NMR spectroscopy, x-ray crystallography, mutagenesis, in vivo functional experiments applied to DsbD, and a comparative sequence analysis of Trx-fold proteins to determine the effect of residues in the vicinity of the active site on the ionization of the key nucleophilic cysteine of the -CXXC- motif. We show that the function and reactivity of Trx-fold proteins depend critically on the electrostatic features imposed by an extended active-site motif.

Original publication




Journal article


J Biol Chem

Publication Date





8681 - 8696


DsbD, Electrostatics, NMR, Oxidase, Reductase, Thiol-Disulfide Exchange, Thioredoxin, Thioredoxin Fold, X-ray Crystallography, pKa Values, Amino Acid Motifs, Amino Acid Sequence, Catalytic Domain, Crystallography, X-Ray, Escherichia coli, Escherichia coli Proteins, Humans, Models, Molecular, Molecular Sequence Data, Oxidoreductases, Point Mutation, Protein Structure, Tertiary, Sequence Alignment, Thioredoxins