Molecular Insights into the Conformational Dynamics of the Novel Dispersion Sensor Histidine Kinase DspS.

and dual-bound forms. Such asymmetry may represent a mechanistic adaptation to fluctuating CDA levels, allowing graded receptor activation under dynamic environmental conditions. MSM analysis further revealed conformational plasticity, showing that full ligand occupancy stabilizes a network of metastable states and enables transitions within an active-like conformational ensemble. These findings provide the first atomistic view of DspS conformational switching, establishing a structural framework to study related histidine kinases and design antivirulence strategies targeting DspS-mediated biofilm control.