Thermodynamics and dynamics of histidine-binding protein, the water-soluble receptor of histidine permease. Implications for the transport of high and low affinity ligands.

@article{Kremer2000ThermodynamicsAD,
  title={Thermodynamics and dynamics of histidine-binding protein, the water-soluble receptor of histidine permease. Implications for the transport of high and low affinity ligands.},
  author={D I Kreĭmer and Henryk Malak and Joseph R. Lakowicz and Sergei Trakhanov and Enrique Villar and Valery Shnyrov},
  journal={European journal of biochemistry},
  year={2000},
  volume={267 13},
  pages={4242-52}
}
The bacterial histidine permease is a model system for ABC transporters (traffic ATPases). The water-soluble receptor of this permease, HisJ, binds L-histidine and L-arginine (tightly) and L-lysine and L-ornithine (less tightly) in the periplasm, interacts with the membrane-bound complex (HisQMP2) and induces its ATPase activity, which results in ligand translocation. HisJ is a two-domain protein; in the absence of ligand, the cleft between two domains is open and binding of substrate… CONTINUE READING

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