Figure 1.

A. Chemical structure and biological activity of the previously optimized inhibitor 8a. [7] IC₅₀ against the Pseudomonas aeruginosa RmlA protein, MIC₁₀₀ against Mycobacterium tuberculosis. The aims of this work were to modify the N¹- and C6-NH₂ positions. B. A representation of 8a bound in the allosteric site of RmlA based on our previous X-ray crystallographic analysis of the RmlA-8a complex [PDB 4ASJ]. Residues that make up the N¹-substituent sub-pocket are highlighted. C. Schematic representation of pocket interactions between 8a and the enzyme showing that the C6-NH₂ in 8a has the tendency to point out of the allosteric pocket into solution.