Structure of the membraneous fumarate sensor DcuS from Escherichia coli

点击翻译按钮获取中文摘要

Two-component regulatory systems represent the most prevalent systems for transmembrane signalling in bacteria. The sensors of these systems consist of a periplasmic ligand binding domain, transmembrane helices and cytoplasmic histidine protein kinases. No structural information on the ligand binding and the transducing transmembrane helices is available. In preparatory work a fumarate sensor DcuS of Escherichia coli has been identified and structural studies of the ligand binding domain have been started by NMR spectroscopy. The two dimensional structure is finished and shows an a3ba2b3 structure, and the fumarate binding region was identified. In the proposal the structure of the ligand binding and of the membrane integral domains will be studied. Understanding the structures and structural changes in both domains in response to ligand binding will help to understand signal preception and transmission into and across the membrane. The structural and functional studies rely on liquid and solid state NMR spectroscopy in combination with molecular biological and biochemical methods in vivo and in vitro.