Reversing allosteric communication: From detecting allosteric sites to inducing and tuning targeted allosteric response
Fig 2
Free energy profiles obtained as a result of the reverse perturbation for AnthS, ATCase, CAP and DAHPS.
(A) AnthS, a heterotetramer involved in the biosynthesis of anthranilate. (B) ATCase, a heterododecamer that catalyzes the first step in pyrimidine biosynthesis. (C) CAP, a homodimeric transcriptional activator. (D) DAHPS, a homotetramer involved in the biosynthesis of aromatic amino acids. The free energy changes are the average from corresponding residues in different subunits. The symbols indicate residues in corresponding ligand binding sites. Grey error bands indicate the standard deviation of Δgi across the subunits. In the middle, the structure of the protein in the Cα coarse-grained model is colored according to the free energy change (increased–blue, decreased–red). The tube radius is proportional to the value of the free energy change. Colored spheres indicate ligand binding sites in a simplified quaternary structure depicted on the right: red or orange colors are used for functional sites, blue–for allosteric sites.