Recognition of peptidoglycan and beta-lactam antibiotics by the extracellular domain of the Ser/Thr protein kinase StkP from Streptococcus pneumoniae

0370932 - MBÚ 2012 RIV GB eng J - Journal Article
Maestro, B. - Nováková, Linda - Hesek, D. - Lee, M. - Leyva, E. - Mobashery, S. - Sanz, J.M. - Branny, Pavel
Recognition of peptidoglycan and beta-lactam antibiotics by the extracellular domain of the Ser/Thr protein kinase StkP from Streptococcus pneumoniae.
FEBS Letters. Roč. 585, č. 2 (2011), s. 357-363. ISSN 0014-5793. E-ISSN 1873-3468
R&D Projects: GA ČR GP204/07/P082; GA ČR GA204/08/0783; GA AV ČR IAA600200801
Institutional research plan: CEZ:AV0Z50200510
Keywords : Signal transduction * Penicillin-binding protein and Ser/Thr protein kinase-associated domain * Peptidoglycan
Subject RIV: CE - Biochemistry
Impact factor: 3.538, year: 2011

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 beta-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 beta-lactam antibiotics.
Permanent Link: http://hdl.handle.net/11104/0204604