Structural highlights
Publication Abstract from PubMed
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.
X-ray structural studies of the entire extra-cellular region of the Ser/Thr kinase PrkC from Staphylococcus aureus.,Ruggiero A, Squeglia F, Marasco D, Marchetti R, Molinaro A, Berisio R Biochem J. 2011 Jan 6. PMID:21208192[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ruggiero A, Squeglia F, Marasco D, Marchetti R, Molinaro A, Berisio R. X-ray structural studies of the entire extra-cellular region of the Ser/Thr kinase PrkC from Staphylococcus aureus. Biochem J. 2011 Jan 6. PMID:21208192 doi:10.1042/BJ20101643
