Structural characterization of substrate and inhibitor binding to farnesyl pyrophosphate synthase from Pseudomonas aeruginosa
The crystal structures of farnesyl diphosphate synthase from the pathogen Pseudomonas aeruginosa in complex with substrates and inhibitors have been determined. The study reveals the presence of an allosteric binding pocket also in bacterial enzymes that, similar to the human enzyme, could be the target for the design of specific and potent inhibitors.