High-resolution structure of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus aureus and characterization of its interaction with the bifunctional HPr kinase/phosphorylase.

@article{Maurer2004HighresolutionSO,
  title={High-resolution structure of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus aureus and characterization of its interaction with the bifunctional HPr kinase/phosphorylase.},
  author={T. Maurer and S. Meier and Norman Kachel and C. Munte and Sonja Hasenbein and B. Koch and W. Hengstenberg and H. Kalbitzer},
  journal={Journal of bacteriology},
  year={2004},
  volume={186 17},
  pages={
          5906-18
        }
}
A high-resolution structure of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus aureus was obtained by heteronuclear multidimensional nuclear magnetic resonance (NMR) spectroscopy on the basis of 1,766 structural restraints. Twenty-three hydrogen bonds in HPr could be directly detected by polarization transfer from the amide nitrogen to the carbonyl carbon involved in the hydrogen bond. Differential line broadening was used to characterize the interaction of HPr with… Expand
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