Journal
FEBS LETTERS
Volume 585, Issue 2, Pages 357-363Publisher
WILEY
DOI: 10.1016/j.febslet.2010.12.016
Keywords
Signal transduction; Penicillin-binding protein and Ser/Thr protein kinase-associated domain; Peptidoglycan; beta-Lactam antibiotics; Protein structure; Streptococcus pneumoniae
Funding
- Spanish Ministry of Education [BIO2007-67304-C02-02, BFU2010-17824]
- European Union [EU-CP223111]
- Czech Science Foundation [204/07/P082, 204/08/0783]
- Grant Agency of the Academy of Sciences of the Czech Republic [IAA600200801]
- National Institutes of Health for the research in the USA
- [AV0Z50200510]
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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. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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