Silencing Cholera's Social Media (IMAGE)

PLOS

Silencing Cholera's Social Media

Caption

Proposed mechanism of LuxO activation and inhibition. Phosphorylation (green) activates LuxO by triggering a conformational change in the R domain that destabilizes the RC interface, dislocating the R-C linker from the LuxO ATP binding site and freeing the ATPase active site for catalysis (denoted by orange ATP). The location and dynamics of the phosphorylated R domains are unknown. Active LuxO uses the energy of ATP hydrolysis to open σ54-dependent promoters, converting them to transcriptionally active states. Active LuxO is also susceptible to competitive inhibition by AzaU or CV-133 (red). Binding of a single inhibitor molecule appears capable of inhibiting the entire ring.

Credit

Boyaci <i>et al</i>.

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