Robinson Lab

The main focus of our research is the study of unique bacterial GTPases that have potential as targets for antimicrobial development. Most bacterial GTPases bind to the ribosome and so a large portion our work is aimed toward understanding this association and how it is influenced by the GTPase activities of the protein. Research projects in the lab span several scientific fields including structural biology, biophysics, biochemistry and bacterial genetics. Interested students are encouraged to talk with Dr. Robinson about their specific areas of interest.

 

We currently have openings for students to work on the following projects:

• Structure/ Function studies of Salmonella typhimurium BipA. BipA is a highly conserved prokaryotic GTPase which functions as a regulator of virulence processes in many strains of globally problematic bacteria. We are using x-ray crystallography as well as other biophysical and biochemical techniques to elucidate the molecular mechanism of action of this protein and how its biophysical properties influence its cellular actions.

• Structure/ Function studies of EngA. EngA is an essential prokaryotic GTPase. It is the only known protein to have in its primary amino acid sequence two tandemly repeated GTP-binding domains (GD1 and GD2). Interestingly, both GD1 and GD2 are needed for proper functioning of EngA in vivo. Ongoing crystallography and biochemistry studies are aimed at uncovering how inter- and intra-domain regulation occurring within the protein and between this protein and its cognate partners.

• Other projects. There are several other GTPase projects ongoing in the lab. Contact Dr. Robinson (victoria.robinson@uconn.edu) for details.