FimV is one of the most challenging proteins we’ve worked on for many reasons, but it is really important for twitching motility in P. aeruginosa. In a very collaborative project involving microbiology, biochemistry, bioinformatics, and structural biology, PhD candidate Ryan Buensuceso and friends showed that a highly conserved segment of the protein at its C-terminus interacts with FimL, an activator of the enzyme that makes cAMP – a small molecule critical to expression of virulence factors. The same region is also responsible for cAMP-independent functions of FimV, making it a good place to target inhibitors. The crystal structure of this region will help in the design of such drugs. Well done everyone!
You can read the paper here.