Crystal structure of Sa239 reveals the structural basis for the activation of ribokinase by monovalent cations.

@article{Li2012CrystalSO,
  title={Crystal structure of Sa239 reveals the structural basis for the activation of ribokinase by monovalent cations.},
  author={Jing Li and Chengliang Wang and Yejuan Wu and Minhao Wu and Lin Wang and Yang Wang and Jianye Zang},
  journal={Journal of structural biology},
  year={2012},
  volume={177 2},
  pages={578-82}
}
Ribokinase is responsible for catalyzing the reaction of d-ribose and ATP to produce ribose-5-phosphate and ADP, which can be activated by monovalent cations such as potassium, cesium and ammonium. However, the exact activation mechanism of ribokinase remains elusive. Here we report the crystal structure of Sa239, a ribokinase from Staphylococcus aureus, in the absence of monovalent ions. In addition to the dimer form similar to that observed in Escherichia coli ribokinase structure, the… CONTINUE READING