The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency.

@article{Darby1998TheMS,
  title={The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency.},
  author={Nigel J Darby and Elke Penka and Renaud Vincentelli},
  journal={Journal of molecular biology},
  year={1998},
  volume={276 1},
  pages={239-47}
}
Protein disulfide isomerase (PDI) catalyzes protein folding linked to disulfide bond formation in secreted proteins. It consists of four major domains, denoted a, b, b' and a'. The a and a' domains each contain an active site motif, -CGHC-, which is directly involved in thiol-disulfide exchange reactions during catalysis. The roles of the b and b' domains and the functional necessity for the multi-domain structure of PDI are unknown. We now demonstrate that full catalytic activity requires the… CONTINUE READING