ATP and magnesium drive conformational changes of the Na+/K+-ATPase cytoplasmic headpiece.

@article{Grycov2009ATPAM,
  title={ATP and magnesium drive conformational changes of the Na+/K+-ATPase cytoplasmic headpiece.},
  author={Lenka Grycov{\'a} and Petr Sklenovsk{\'y} and Zdenek Lansky and Marika Janovsk{\'a} and Michal Otyepka and Ev{\vz}en Amler and Jan Teisinger and Martin Kubala},
  journal={Biochimica et biophysica acta},
  year={2009},
  volume={1788 5},
  pages={1081-91}
}
Conformational changes of the Na(+)/K(+)-ATPase isolated large cytoplasmic segment connecting transmembrane helices M4 and M5 (C45) induced by the interaction with enzyme ligands (i.e. Mg(2+) and/or ATP) were investigated by means of the intrinsic tryptophan fluorescence measurement and molecular dynamic simulations. Our data revealed that this model system consisting of only two domains retained the ability to adopt open or closed conformation, i.e. behavior, which is expected from the crystal… CONTINUE READING

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