Fig. 4: F1P-induced structural dynamics of FruR.

A Root mean square deviation (RMSD) values of the structures observed during 90 ns of molecular dynamics (MD) simulations were compared between FruR structures in the presence (red) and absence (black) of F1P. B Structural modifications were observed throughout the time-course analysis. Ribbon diagrams of FruR structures at 20 ns (orange) and 80 ns (green) time points for both apo FruR (left) and the F1P-FruR complex (right) were aligned using PyMOL for comparison. F1P is colored red for visualization. The N-terminal DNA binding domain and C-terminal sensor domain are indicated within white boxes. The black arrow highlights the structural change in the N-terminal DNA binding domain. C Fluorescence quenching was measured as described in the “Methods” section. FruR and FruR mutants were mixed with varying concentrations of FBP or F1P (0 mM; black, 0.1 mM; orange, 0.5 mM; red) to assess the degree of fluorescence quenching.