X-ray structural studies of the entire extra-cellular region of the Ser/Thr kinase PrkC from Staphylococcus aureus

Alessia Ruggiero , Flavia Squeglia , Daniela Marasco , Roberta Marchetti , Antonio Molinaro , Rita Berisio (1)

1 IBB - Institute of biostructures and bioimaging

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.

Mots clés: Life Sciences

Alessia Ruggiero, Flavia Squeglia, Daniela Marasco, Roberta Marchetti, Antonio Molinaro, et al.. X-ray structural studies of the entire extra-cellular region of the Ser/Thr kinase PrkC from Staphylococcus aureus. Biochemical Journal, 2011, 435 (1), pp.33-41. ⟨10.1042/BJ20101643⟩. ⟨hal-00576990⟩