Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization.

@article{Guddat1998CrystalSO,
  title={Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization.},
  author={Luke W. Guddat and James C. A. Bardwell and Jennifer L. Martin},
  journal={Structure},
  year={1998},
  volume={6 6},
  pages={757-67}
}
BACKGROUND The redox proteins that incorporate a thioredoxin fold have diverse properties and functions. The bacterial protein-folding factor DsbA is the most oxidizing of the thioredoxin family. DsbA catalyzes disulfide-bond formation during the folding of secreted proteins. The extremely oxidizing nature of DsbA has been proposed to result from either domain motion or stabilizing active-site interactions in the reduced form. In the domain motion model, hinge bending between the two domains of… CONTINUE READING

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