A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor.

@article{Kurokawa2004ARM,
  title={A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor.},
  author={Hirofumi Kurokawa and D Lee and Miki Watanabe and Ikuko Sagami and Bunzo Mikami and C. S. Raman and Toru Shimizu},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 19},
  pages={20186-93}
}
PAS domains, which have been identified in over 1100 proteins from all three kingdoms of life, convert various input stimuli into signals that propagate to downstream components by modifying protein-protein interactions. One such protein is the Escherichia coli redox sensor, Ec DOS, a phosphodiesterase that degrades cyclic adenosine monophosphate in a redox-dependent manner. Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at… CONTINUE READING