RT Journal Article
T1 Recognition of peptidoglycan and beta-lactam antibiotics by the extracellular domain of the Ser/Thr protein kinase StkP from Streptococcus pneumoniae
A1 Maestro García-Donas, María Beatriz
A1 Novakova, L.
A1 Hesek, D.
A1 Lee, M.
A1 Leyva, E.
A1 Mobashery, S.
A1 Sanz, J. M.
A1 Branny, P.
AB The 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.
PB Wiley
SN 0014-5793
YR 2010
FD 2010-12-15
LK https://hdl.handle.net/20.500.14352/93182
UL https://hdl.handle.net/20.500.14352/93182
LA eng
NO Unión Europea
NO Czech Science Foundation
NO Agency of the Academy of Sciences of the Czech Republic
NO Institutional Research Concept
NO National Institutes of Health for the research in the USA
DS Docta Complutense
RD 10 abr 2025