The extended conformation of the 2.9-Å crystal structure of the three-PASTA domain of a Ser/Thr kinase from the human pathogen Staphylococcus aureus.

@article{Paracuellos2010TheEC,
  title={The extended conformation of the 2.9-{\AA} crystal structure of the three-PASTA domain of a Ser/Thr kinase from the human pathogen Staphylococcus aureus.},
  author={Patricia Paracuellos and Allison Ballandras and Xavier Robert and Richard Kahn and Mireille Herv{\'e} and Dominique Mengin-Lecreulx and Alain J. Cozzone and Bertrand Duclos and Patrice Gouet},
  journal={Journal of molecular biology},
  year={2010},
  volume={404 5},
  pages={
          847-58
        }
}
PASTA (penicillin-binding protein and serine/threonine kinase associated) modules are found in penicillin-binding proteins and bacterial serine/threonine kinases mainly from Gram-positive Firmicutes and Actinobacteria. They may act as extracellular sensors by binding peptidoglycan fragments. We report here the first crystal structure of a multiple-PASTA domain from Ser/Thr kinase, that of the protein serine/threonine kinase 1 (Stk1) from the Firmicute Staphylococcus aureus. The extended… CONTINUE READING
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The

  • P. Barthe, G. V. Mukamolova, C. Roumestand, M. Cohen-Gonsaud
  • structure
  • 2010