Figure 5. Altered conformational dynamics of PKA-C^E31V revealed by MD simulations.

(A) ΔRMSF of PKA-C^E31V in the binary form over 1.0 μs of simulation. (B) Overlay of PKA-C^WT (PDB: 1ATP; gray) and PKA-C^E31V (from MD simulations; red) highlighting the structural rearrangements of the αA- and αC-helices caused by the E31V mutation. The inset shows the cation-π stacking interactions altered in response to the mutation. (C) Distinct dynamics of the pseudosubstrate, PKI_5–24, in the ternary complex. Putty representation of RMSF for PKI_5–24 for a typical MD snapshot of PKA-C^WT (gray) and PKA-C^E31V (red). (D)Comparison of allosteric mapping from mutual information matrices (MI_cutoff = 0.3), with the key hub residues labeled for PKA-C^WT (right) and PKA-C^E31V (left).