Thiol-disulfide exchange in an immunoglobulin-like fold: structure of the N-terminal domain of DsbD.

@article{Goulding2002ThioldisulfideEI,
  title={Thiol-disulfide exchange in an immunoglobulin-like fold: structure of the N-terminal domain of DsbD.},
  author={Celia W Goulding and Michael R. Sawaya and Angineh Parseghian and Vincent Lim and David S Eisenberg and Dominique Missiakas},
  journal={Biochemistry},
  year={2002},
  volume={41 22},
  pages={6920-7}
}
Escherichia coli DsbD transports electrons across the plasma membrane, a pathway that leads to the reduction of protein disulfide bonds. Three secreted thioredoxin-like factors, DsbC, DsbE, and DsbG, reduce protein disulfide bonds whereby an active site C-X-X-C motif is oxidized to generate a disulfide bond. DsbD catalyzes the reduction of the disulfide of DsbC, DsbE, and DsbG but not of the thioredoxin-like oxidant DsbA. The reduction of DsbC, DsbE, and DsbG occurs by transport of electrons… CONTINUE READING

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  • C. W. Goulding, A. Parseghian, M. Gennaro, D. Eisenberg
  • 2002

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