Fig. 1: Generation of allosteric variants of ATP-PRT. | Nature Communications

Fig. 1: Generation of allosteric variants of ATP-PRT.

From: Activation of l-histidine biosynthesis as a new antibiotic strategy against Mycobacterium tuberculosis

Fig. 1: Generation of allosteric variants of ATP-PRT.

A Overall reaction catalyzed by ATP-PRT. B Scheme illustrating the 3-dimensional structure of M. tuberculosis ATP-PRT in open and closed (l-histidine bound) conformations (PDB ID 1NH7 and 5LHU, respectively). The catalytic domain is shown in blue, and the allosteric domain is in gold. C Scheme of the allosteric site of M. tuberculosis ATP-PRT with l-histidine bound, illustrating the residues chosen for mutagenesis. D Amino acid occurrence at the six positions identified in panel (C). E Thermodynamic stability (expressed as the fraction of enzyme unfolded - fU) of ATP-PRT wild-type (black traces) and variants (red traces) in the absence (solid line) and presence (dashed) of l-histidine. Lines represent the fit of the data. The data are representative of two independent experiments.

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