New publication about the mechanism of sensor kinase CitA transmembrane signaling

Mechanism of sensor kinase CitA transmembrane signaling

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.