Maestro García-Donas, María BeatrizNovakova, LindaHesek, DusanLee, MijooLeyva, EduardoMobashery, ShahriarSanz, JesúsBranny, Pavel2024-01-232024-01-152024-01-232010Maestro, Beatriz, et al. «Recognition of Peptidoglycan and β-Lactam Antibiotics by the Extracellular Domain of the Ser/Thr Protein Kinase StkP from Streptococcus Pneumoniae». FEBS Letters, vol. 585, n.o 2, enero de 2011, pp. 357-63. https://doi.org/10.1016/j.febslet.2010.12.016.0014-579310.1016/j.febslet.2010.12.016https://hdl.handle.net/20.500.14352/93182.2The 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.engAttribution 4.0 Internationalhttp://creativecommons.org/licenses/by/4.0/journal article1873-3468https://doi.org/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