Heme ligand binding properties and intradimer interactions in the full-length sensor protein dos from Escherichia coli and its isolated heme domain.

@article{Lechauve2009HemeLB,
  title={Heme ligand binding properties and intradimer interactions in the full-length sensor protein dos from Escherichia coli and its isolated heme domain.},
  author={Christophe Lechauve and Latifa Bouzhir-Sima and Taku Yamashita and M C Michael C Marden and Marten H Vos and Ursula Liebl and Laurent Kiger},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 52},
  pages={36146-59}
}
Dos from Escherichia coli is a bacterial gas sensor protein comprising a heme-containing gas sensor domain and a phosphodiesterase catalytic domain. Using a combination of static light scattering and gel filtration experiments, we established that, as are many other sensor proteins, the full-length protein is dimeric. The full-length dimer (association constant <10 nm) is more stable than the dimeric heme domain (association constant approximately 1 mum), and the dimer interface presumably… CONTINUE READING