High-resolution structures of Escherichia coli cDsbD in different redox states: A combined crystallographic, biochemical and computational study.

@article{Stirnimann2006HighresolutionSO,
  title={High-resolution structures of Escherichia coli cDsbD in different redox states: A combined crystallographic, biochemical and computational study.},
  author={Christian U. Stirnimann and A. Yu. Rozhkova and Ulla Grauschopf and Rainer A. B{\"o}ckmann and Rudi Glockshuber and Guido Capitani and Markus G. Gruetter},
  journal={Journal of molecular biology},
  year={2006},
  volume={358 3},
  pages={
          829-45
        }
}
Escherichia coli DsbD transports electrons from cytoplasmic thioredoxin to periplasmic target proteins. DsbD is composed of an N-terminal (nDsbD) and a C-terminal (cDsbD) periplasmic domain, connected by a central transmembrane domain. Each domain possesses two cysteine residues essential for electron transport. The transport proceeds via disulfide exchange reactions from cytoplasmic thioredoxin to the central transmembrane domain and via cDsbD to nDsbD, which then reduces the periplasmic… CONTINUE READING

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