Solution structure of the PAS domain of a thermophilic YybT protein homolog reveals a potential ligand-binding site.

@article{Tan2013SolutionSO,
  title={Solution structure of the PAS domain of a thermophilic YybT protein homolog reveals a potential ligand-binding site.},
  author={Edward Tan and Feng Rao and Swathi Pasunooti and Thi Lam Huong Pham and Ishin Soehano and Mark S Turner and Chong Wai Liew and Julien Lescar and Konstantin Pervushin and Zhao-Xun Liang},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 17},
  pages={11949-59}
}
The Bacillus subtilis protein YybT (or GdpP) and its homologs were recently established as stress signaling proteins that exert their biological effect by degrading the bacterial messenger cyclic di-AMP. YybT homologs contain a small Per-ARNT-Sim (PAS) domain (~80 amino acids) that can bind b-type heme with 1:1 stoichiometry despite the small size of the domain and the lack of a conserved heme iron-coordinating residue. We determined the solution structure of the PAS domain of GtYybT from… CONTINUE READING
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