X-ray structure of HPr kinase: a bacterial protein kinase with a P-loop nucleotide-binding domain.

@article{Fieulaine2001XraySO,
  title={X-ray structure of HPr kinase: a bacterial protein kinase with a P-loop nucleotide-binding domain.},
  author={Sonia Fieulaine and Solange Mor{\'e}ra and Sandrine Poncet and Vicente Monedero and Virginie Gueguen-Chaignon and Anne Galinier and Jo{\"e}l Janin and Josef Deutscher and Sylvie Nessler},
  journal={The EMBO journal},
  year={2001},
  volume={20 15},
  pages={3917-27}
}
HPr kinase/phosphatase (HprK/P) is a key regulatory enzyme controlling carbon metabolism in Gram- positive bacteria. It catalyses the ATP-dependent phosphorylation of Ser46 in HPr, a protein of the phosphotransferase system, and also its dephosphorylation. HprK/P is unrelated to eukaryotic protein kinases, but contains the Walker motif A characteristic of nucleotide-binding proteins. We report here the X-ray structure of an active fragment of Lactobacillus casei HprK/P at 2.8 A resolution… CONTINUE READING

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