Eigenvector centrality difference associated with binding of PRFAR effector (holo enzyme) at 30 °C (left) or 50 °C (right) and with a temperature increase in the apo IGPS enzyme (middle). Secondary structures with increased (in red) or decreased (in blue) centralities are analogous upon effector binding or temperature increase in both HisF and HisH units of IGPS. Secondary structures mainly involved in the temperature- and effector-induced allosteric communication network (positive differential centralities, in red) are located at sideR, including loop1, f α2, f α3 in HisF and h α1 in HisH. The effector binding at high temperature (50 °C) features much fewer specific communication pathways than at 30 °C.
