Comparison of specific mutual information pathways connecting the PRFAR phosphate binding sites (residues f T104 and f A224 in HisF, red spheres located in sideL and sideR) to the active site (h G50 in HisH, red sphere). Secondary structure elements involved in the shortest communication pathways are highlighted, separating contributions of surface (solvent-exposed) amino acids (“external”, in yellow) from those buried in the protein (“internal”, in green). The information pathways in the allosterically inactive apo enzyme at 30 °C (apo30) differ from those of the IGPS activated by a temperature increase (apo50) or by effector binding (holo30), which instead feature some similarities. Source data are provided as a Source Data file.
