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Recognition of peptidoglycan and β‐lactam antibiotics by the extracellular domain of the Ser/Thr protein kinase StkP from Streptococcus pneumoniae
Author(s) -
Maestro Beatriz,
Novaková Linda,
Hesek Dusan,
Lee Mijoon,
Leyva Eduardo,
Mobashery Shahriar,
Sanz Jesús M.,
Branny Pavel
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.12.016
Subject(s) - peptidoglycan , streptococcus pneumoniae , kinase , extracellular , protein kinase domain , biochemistry , signal transduction , protein kinase a , threonine , biology , serine , antibiotics , chemistry , cell wall , microbiology and biotechnology , phosphorylation , gene , mutant
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.