X-ray structural studies of the entire extra-cellular region of the Ser/Thr kinase PrkC from Staphylococcus aureus
Résumé
Bacterial Ser/Thr kinases modulate a wide number of cellular processes. PrkC kinase from human pathogen Staphylococcus aureus was also shown to induce germination of Bacillus subtilis spores, in response to cell-wall muropeptides. The presence of muropeptides in the bacterial extra-cellular milieu is a strong signal that growing conditions are promising. We report here the x-ray structure of the entire extra-cellular region of PrkC from Staphylococcus aureus. This structure reveals that the extra-cellular region of PrkC, EC-PrkC, is a linear modular structure, composed of three PASTA domains and an unpredicted C-terminal domain, which presents the typical features of adhesive proteins. Using several solution techniques, we also evidenced that EC-PrkC shows no tendency to dimerise even in the presence of high concentrations of muropeptides. X-ray structural results obtained here provide molecular clues into the mechanism of muropeptide-induced PrkC activation.
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