Our paper entitled “Mechanism of sensor kinase CitA transmembrane signaling” has been published in Nature Communications.
We have employed an integrated structural biology approach combining solid-state NMR, crystallography, solution NMR, and distance measurements to elucidate the transmembrane signaling mechanism of the membrane-bound histidine kinase CitA. Central to our study is the application of COLD (Cryogenic Optical Localization in 3D) microscopy, which enables high-precision measurement of conformational dynamics in membrane-embedded proteins. By targeting site-specific labeling within the cytosolic PAS domain, we resolve nanometer-scale rearrangements induced by extracellular citrate binding. Our results reveal a piston-like displacement of transmembrane helix 2 coupled to a dimeric conformational switch in the cytosolic PAS domain, providing a structural framework for signal transmission across bacterial membranes.
Read our publication here.