Fig. 2

Sequence and structure analysis of wild-type FolC and mutants. A Sequence alignment of FolC orthologs in mycobacterial species. Magenta triangles indicated the position of mutants found in our study. FolC_MTB, FolC from MTB (UniProt entry I6Y0R5); FolC_Eco, FolC from E. coli (UniProt entry P08192); FolC_Hin, FolC from H. influenzae (UniProt entry P43775); FolC_Bsu, FolC from B. subtilis (UniProt entry Q05865). B Three-dimensional structure of wild-type MTB FolC in complex with DHP-P and ADP. The LeuRS protein (cyan) was displayed in cartoon mode. The six different residues (magenta) were shown as sticks. Ligands DHP-P (yellow), ADP (red) and magnesium ions (green) were represented in CPK mode. C, D The 2D diagram showing the interactions between wild-type FolC and DHP-P (C) and ADP (D). The ligand molecules, namely DHP-P and ADP, were shown in the middle with a display style of ball and stick. The colored balls indicated the residues involved in the direct interactions between FolC and ligand. The green, purple and yellow dash line connecting ligand and corresponding residue indicated intermolecular hydrogen bond, hydrophobic interaction and attractive charge, respectively. Residues involved in hydrogen bond, van der Waals interactions or polar interactions were represented by green balls. Residues involved hydrophobic interactions and attractive charge were displayed by purple and orange balls, respectively