LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Homologous_superfamily |
| Description | This superfamily represents the N-terminal domain of the disulphide bond isomerase DsbC and DsbG.The disulphide bond isomerase (DsbC) is one of five Escherichia coli 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 [ ]. 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 α-β(4) core, where the helix packs against the coiled antiparallel β-sheet [].It has been suggested that DsbG functions as a disulfide isomerase with a narrower substrate specificity than DsbC. |
| Short Name | DiS-bond_isomerase_DsbC/G_N_sf |
