Antioxidant Dps protein from the thermophilic cyanobacterium Thermosynechococcus elongatus.

@article{Franceschini2006AntioxidantDP,
  title={Antioxidant Dps protein from the thermophilic cyanobacterium Thermosynechococcus elongatus.},
  author={Stefano Franceschini and Pierpaolo Ceci and Flaminia Alaleona and Emilia Chiancone and Andrea Ilari},
  journal={The FEBS journal},
  year={2006},
  volume={273 21},
  pages={4913-28}
}
DNA-binding proteins from starved cells (Dps proteins) protect bacteria primarily from oxidative damage. They are composed of 12 identical subunits assembled with 23-symmetry to form a compact cage-like structure known to be stable at temperatures > 70 degrees C and over a wide pH range. Thermosynechococcus elongatus Dps thermostability is increased dramatically relative to mesophilic Dps proteins. Hydrophobic interactions at the dimeric and trimeric interfaces called Dps-like are replaced by… CONTINUE READING