Mutational analysis of the connector segment in the HAMP domain of Tsr, the Escherichia coli serine chemoreceptor.

@article{Ames2008MutationalAO,
  title={Mutational analysis of the connector segment in the HAMP domain of Tsr, the Escherichia coli serine chemoreceptor.},
  author={Peter Ames and Qin Zhou and J. S. Parkinson},
  journal={Journal of bacteriology},
  year={2008},
  volume={190 20},
  pages={6676-85}
}
HAMP domains are approximately 50-residue motifs, found in many bacterial signaling proteins, that consist of two amphiphilic helices joined by a nonhelical connector segment. The HAMP domain of Tsr, the serine chemoreceptor of Escherichia coli, receives transmembrane input signals from the periplasmic serine binding domain and in turn modulates output signals from the Tsr kinase control domain to elicit chemotactic responses. We created random amino acid replacements at each of the 14… CONTINUE READING