Dynamic Allostery of the Catabolite Activator Protein Revealed by Interatomic Forces
Fig 3
Allosteric network upon binding the first cAMP obtained from FDA.
Residue pairwise forces difference between the apo and the cap1 states are shown as blue sticks at a 50 pN (A) and 40 pN cut-off (B) for the CAP homo-dimer represented as cartoon. The first and second protomers are depicted in white and yellow, respectively. The cAMP molecule (white) and key residues are represented as sticks. (C, D) Zoom of (B) to highlight two distinct allosteric connection pathways termed A (C) and B (D) in the allosteric network between the two protomers at a cut-off value of 40 pN. Note that D is rotated by 180 degrees with respect to C.