Fig. 5: Effect of PaHisZ binding on PaHisGS dynamic network. | Nature Communications

Fig. 5: Effect of PaHisZ binding on PaHisGS dynamic network.

From: Allosteric rescue of catalytically impaired ATP phosphoribosyltransferase variants links protein dynamics to active-site electrostatic preorganisation

Fig. 5

a SPM analysis of nonactivated PaHisGS dimer. b SPM analysis of activated PaHisGS dimer upon PaHisZ binding (only the catalytic subunits are shown). c SPM analysis of PaATPPRT including PaHisZ residues. d Side view (90° rotation) of c. PaHisGS monomers are shown in light and dark teal, while PaHisZ is shown in pink. The histidine-binding loop (D256 – I269) is shown in yellow in d. The sizes of the edges (black lines) and vertices (spheres) indicate the strength of the network (the larger size the more pathways available, and thus the higher the importance for allosteric communication). The positions of key residues in the histidine-binding loop and some included in the node-weakening analysis are denoted by arrows; if they are adjacent to the SPM, the number in brackets indicates how many amino-acid residues away they are from the closest residue encompassed by the SPM.

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