High-affinity inhibitors of Zymomonas mobilis tRNA-guanine transglycosylase through convergent optimization

The simultaneous filling of the ribose-33 and ribose-34 pockets at the active site of Z. mobilis tRNA-guanine transglycosylase was investigated using a series of bifunctionalized lin-benzopurine inhibitors. A strong influence of the crystallization protocol on the solvation pattern and the residual mobility of the bound ligands was observed in the cocrystal structures.