Solution structure of NPr, a bacterial signal-transducing protein that controls the phosphorylation state of the potassium transporter-regulating protein IIANtr

@article{Li2008SolutionSO,
  title={Solution structure of NPr, a bacterial signal-transducing protein that controls the phosphorylation state of the potassium transporter-regulating protein IIANtr},
  author={Xia Chong Li and Alan Peterkofsky and Guangshun Wang},
  journal={Amino Acids},
  year={2008},
  volume={35},
  pages={531-539}
}
A nitrogen-related signal transduction pathway, consisting of the three phosphotransfer proteins EINtr, NPr, and IIANtr, was discovered recently to regulate the uptake of K+ in Escherichia coli. In particular, dephosphorylated IIANtr inhibits the activity of the K+ transporter TrkA. Since the phosphorylation state of IIANtr is partially determined by its reversible phosphorylation by NPr, we have determined the three-dimensional structure of NPr by solution NMR spectroscopy. In total, we… CONTINUE READING

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Solution structure of Ca 2 + - calmodulin reveals flexible hand - like properties of its domains

  • T Cierpicki, J Otlewski
  • Nat Struct Biol
  • 2001
Highly Influential
1 Excerpt

PROCHECK: a program to check the stereochemical quality of protein structure

  • RA Laskowski, MW MacArthur, DS Moss, JM Thornton
  • J Appl Cryst
  • 1993
Highly Influential
2 Excerpts

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