Fig. 3: NM102 specifically binds the ATP binding site of Mfd. | Nature Communications

Fig. 3: NM102 specifically binds the ATP binding site of Mfd.

From: An anti-virulence drug targeting the evolvability protein Mfd protects against infections with antimicrobial resistant ESKAPE pathogens

Fig. 3

A NM102 inhibition of bacterial Mfd and eukaryotic proteins (ERCC3, ERCC6, XPD, yUpf1) ATPase activity. ATPase activity of the proteins, in the absence and presence of 100 µM of NM102, was assessed by using BIOMOL® Green reagent microtiter-plate assay. Data were normalized to that of the DMSO control. The graph shows the mean of at least two independent experiments with standard deviation. B Michaelis Menten plot for inhibition activity of NM102 (0 to 100 µM) on E. coli RecG (0.35 µM) ATPase activity with ATP (0 to 0.3 mM). The results are the average of two independent experiments done in duplicate with standard deviation. C Binding energy measured in silico in kcal/mol between ATP or NM102 and Mfd (left) anf Upf1 (right). The bindings of ATP and NM102 are shown in cyan, and orange, respectively. The graph shows the distribution of binding energies obtained for twenty poses of the substrate/ligand couple by AutoDock. Source data are provided as a source data file.

Back to article page