Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10872324 | FEBS Letters | 2011 | 7 Pages |
Abstract
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.
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Authors
Beatriz Maestro, Linda Novaková, Dusan Hesek, Mijoon Lee, Eduardo Leyva, Shahriar Mobashery, Jesús M. Sanz, Pavel Branny,