March 15, Tue 2011
2:00 pm, MRB 100 Conference Room
Dr. Mark Fisher
Department of Biochemistry and Molecular Biology, University of Kansas Medical Center
Using the Chaperonin GroEL beyond Protein Folding
In this talk, I will discuss our use of the chaperonin GroEL as a general binding platform to rapidly identify ligands and solution conditions that stabilize that stabilizes a wide range of target proteins. Accordingly, we have also used the chaperonin as a molecule scaffold to capture and stabilize the aggregation-prone membrane-insertion competent form of the Anthrax toxin pore translocation complex for EM structural analysis. We have expanded this scaffold approach to construct the first three dimensional structure of a membrane protein, the anthrax toxin pore, inserted into a ~ 100 Å lipid nanodisc.