肺炎链球菌丝氨酸/苏氨酸蛋白激酶 StkP 的细胞外结构域对肽聚糖和β-内酰胺类抗生素的识别。
Recognition of peptidoglycan and β-lactam antibiotics by the extracellular domain of the Ser/Thr protein kinase StkP from Streptococcus pneumoniae.
机构信息
Instituto de Biologia Molecular y Celular, Universidad Miguel Hernández, Elche, Spain.
出版信息
FEBS Lett. 2011 Jan 21;585(2):357-63. doi: 10.1016/j.febslet.2010.12.016. Epub 2010 Dec 15.
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.
摘要
肺炎链球菌中的真核丝氨酸/苏氨酸激酶 StkP 是一种重要的信号转导元件，可调节许多肺炎链球菌基因的表达。我们已经表达了 StkP 激酶的胞外 C 端结构域（C-StkP），详细阐述了其三维结构模型，并对其结构和稳定性进行了光谱学表征。生物物理实验表明，C-StkP 与细胞壁肽聚糖（PGN）的合成样本以及β-内酰胺抗生素结合，这些抗生素模拟了 PGN 茎肽的末端部分。这是第一个关于含有 PASTA 的激酶识别最小 PGN 单元的实验报告，表明未交联的 PGN 可能作为 StkP 功能的信号，表明该蛋白是β-内酰胺抗生素的一个有趣靶点。
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