Maestro García-Donas, María BeatrizNovakova, L.Hesek, D.Lee, M.Leyva, E.Mobashery, S.Sanz, J. M.Branny, P.2024-01-152024-01-152010-12-150014-579310.1016/j.febslet.2010.12.016https://hdl.handle.net/20.500.14352/93182The eukaryotic-type serine/threonine kinase StkP from Streptococcus pneumoniae is an important signal-transduction element that regulates the expression of numerous pneumococcal genes. We have expressed the extracellular C-terminal domain of StkP kinase (C-StkP), elaborated a three-dimensional structural model and performed a spectroscopical characterization of its structure and stability. Biophysical experiments show that C-StkP binds to synthetic samples of the cell wall peptidoglycan (PGN) and to β-lactam antibiotics, which mimic the terminal portions of the PGN stem peptide. This is the first experimental report on the recognition of a minimal PGN unit by a PASTA-containing kinase, suggesting that non-crosslinked PGN may act as a signal for StkP function and pointing to this protein as an interesting target for β-lactam antibiotics.engjournal article1873-3468https://febs.onlinelibrary.wiley.com/doi/full/10.1016/j.febslet.2010.12.016open access577.1Signal transductionPenicillin-binding protein and Ser/Thrprotein kinase-associated domainPeptidoglycanb-Lactam antibioticsProtein structureStreptococcus pneumoniaeBioquímica (Química)2403 Bioquímica