Fig. 3: Allosteric activation of PaHisGS variants by AbHisZ. | Nature Communications

Fig. 3: Allosteric activation of PaHisGS variants by AbHisZ.

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

Fig. 3

a Dependence of rate of reaction catalysed by PaHisGS variants on the concentration of AbHisZ. Data are the mean of two independent measurements. Best fit of the data to Eq. (3) is shown as a solid line. Best fit of the data to Eq. (5) is shown as a dashed line. Source data are provided as a Source Data file. b Substrate saturation curves for WT-PaHisGS/AbHisZ and R56A-PaHisGS/AbHisZ. Data are the mean of two independent measurements. Lines are best fit of the data to Eq. (1). WT-PaHisGS/AbHisZ concentration was calculated from the KD for AbHisZ with Eq. (4), while R56A-PaHisGS/AbHisZ concentration was assumed to be the same as R56A-PaHisGS in the presence of 26 μM AbHisZ. Source data are provided as a Source Data file. c The crystal structure of PaATPPRT28 (PDB ID 5M8H) viewed from above the PaHisGS dimer. PaHisGS (orange) and PaHisZ (blue) are in surface rendering. The Cα atoms of specific PaHisZ residues at the interface with PaHisGS are shown as spheres, with pink depicting identical residues to AbHisZ, blue depicting residues with similar properties to those in AbHisZ, and green, those not conserved in AbHisZ.

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