期刊
CHEMISTRY & BIOLOGY
卷 20, 期 11, 页码 1411-1420出版社
CELL PRESS
DOI: 10.1016/j.chembiol.2013.09.008
关键词
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资金
- ISMB Wellcome Trust
- Biotechnology and Biological Sciences Research Council [1104644] Funding Source: researchfish
In a commonly accepted model, in response to stimuli, bacterial histidine kinases undergo a conformational transition between an active and inactive form. Structural information on histidine kinases is limited. By using ion mobility-mass spectrometry (IM-MS), we demonstrate an exchange between two conformational populations of histidine kinase ExsG that are linked to different levels of kinase activity. ExsG is an atypical signaling protein that incorporates an uncommon histidine kinase catalytic core at the C terminus preceded by an N-terminal receiver domain that is normally associated with the response regulator proteins in two-component signal transduction systems. IM-MS analysis and enzymatic assays indicate that phosphorylation of the ExsG receiver domain stabilizes the compact form of the protein and inhibits kinase core activity; in contrast, nucleotide binding required for kinase activity is associated with the more open conformation of ExsG.
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