Using cryo-electron microscopy to uncover the atomic structures of dynamic enzyme polymers

Abstract:
Many enzymes in metabolism form large-scale polymers in cells and tissues. These supermolecular structures are critically important for regulating enzyme activity and maintaining cellular function, and their discovery has opened a new field focused on the physical organization of metabolic activity inside cells. Our lab has been working to understand the structural basis for metabolic filament assembly and the biochemical and physiological consequences of enzyme polymerization. Combining cryoEM and functional studies, we have shown that polymerization generally functions as a mechanism for allosteric control of enzyme activity. Here, I will focus on our use of advanced cryo-EM techniques to investigate the near-atomic resolution structures of enzyme polymers.

Bio:
Justin Kollman received his PhD in Biology from UC San Diego in 2005, where he worked on crystal and cryo-EM structures of blood clotting proteins in the lab Prof. Russell Doolittle.  In his postdoctoral work at UC San Francisco with Prof. David Agard he determined the structures of microtubule nucleating complexes using cryo-EM.  He started the lab in the Dept. of Anatomy & Cell BIology at McGill University in 2012, then moved the lab to the Biochemistry Department at the University of Washington in 2014. His lab primarily focuses on the structural biology of enzyme assemblies in intermediate metabolism.