Structures and dynamics of the Hsp90 machinery

Project Summary

Homodimers of the molecular chaperone heat-shock protein 90 (Hsp90) together with the cell division cycle protein 37 (Cdc37) form a protein machinery that is responsible for the chaperoning of most cellular kinases. During processing of these kinases, the machinery forms various dynamic modular assemblies. We will use single molecule Förster resonance energy transfer to address, how the dynamics within the Hsp90-Cdc37 complexes achieve a controlled chaperoning of kinases and how the energy of ATP hydrolysis within Hsp90 is utilized to drive the dynamic multi-protein assembly cycle.