<p>The disulphide bond isomerase (DsbC) is one of five <taxon tax_id="562">Escherichia coli</taxon> proteins required for disulphide bond formation, and functions to rearrange incorrect disulphide bonds during oxidative protein folding in the periplasm. DsbC acts as a homodimer with both disulphide isomerase and chaperone activity. It is selectively activated by the transmembrane electron transporter DsbDalpha, which functions as a thiol oxireductase [<cite idref="PUB00013257"/>]. Like other Dsb proteins, DsbC contains active site Cys-X-X-Cys sequences that form disulphide bonds, characteristic of thioredoxin proteins. DbsC consists of thioredoxin-like domains joined by a flexible hinge region to an N-terminal dimerisation domain. The crystal structure of the N-terminal domain reveals an alpha-beta(4) core, where the helix packs against the coiled antiparallel beta-sheet [<cite idref="PUB00013324"/>].</p> Disulphide bond isomerase, DsbC, N-terminal