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The interdomain contacts observed in the crystal structure of S. cerevisiae imidazole glycerol phosphate synthase and a network of amino acids that mediate the [(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) binding signal to the glutaminase active site is analyzed. The amino acids, D359 from the cyclase domain, and K196, a residue adjacent to the glutaminase active site, form the only conserved interdomain salt bridge in the interface region.

The mechanism of allosteric regulation in imidazole glycerol phosphate (IGP) synthase is probed by combining equilibrium and steered molecular dynamics (SMD) simulations with principal component correlation analyses. Analyses of IGP synthase disclosed a conserved network of interactions leading from the effector-binding site to the glutaminase active site.