Publication | Open Access
Sensory domain contraction in histidine kinase CitA triggers transmembrane signaling in the membrane-bound sensor
32
Citations
39
References
2017
Year
Proteinlipid InteractionMolecular BiologyHistidine Kinase CitaMembrane-bound SensorCellular PhysiologyReceptor Tyrosine KinaseSignificance Histidine KinasesCellular Regulatory MechanismIntercellular CommunicationCell SignalingBiophysicsCell PhysiologySensory Domain ContractionMolecular PhysiologyBiochemistryCitrate BindingBiochemical InteractionMembrane BiologyBiomolecular InteractionProtein TransportSolution Nmr SpectroscopyCell BiologySignal TransductionNatural SciencesCellular BiochemistryMedicine
Significance Histidine kinases are key players in prokaryotic environment sensing. Citrate binding to the extracytoplasmic sensing domain of histidine kinase CitA triggers a contraction of the domain, resulting in a pull on the C-terminal β-strand. By a combination of liquid- and solid-state NMR spectroscopy, structural alterations observed for the isolated domain can be confirmed in context of its native environment as part of a membrane-embedded receptor. Our results demonstrate that the mechanistic model derived from the isolated ligand-sensing domain is compatible with the sensor in a native-like membrane environment and allows transfer of the model to transmembrane signaling by this class of sensor kinases.
| Year | Citations | |
|---|---|---|
Page 1
Page 1