Motor mechanism of native ATPase complexes

• Applicant: Professorin Dr. Petra Wendler
• Subject Area: Structural Biology
• Term: from 2009 to 2015
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 122511187

ATPases of the AAA+ superfamily (ATPases associated with various cellular activities) are often at the core of multi-protein complexes responsible for timely destruction or remodeling of macromolecules in an energy dependent manner. They form one of the largest protein superfamilies and are crucial components in most re-organization and recycling processes of protein, membrane or DNA within the cell. Their unique functional specificity derives from combining the highly conserved AAA+ domain with accessory domains and proteins which facilitate fine tuning of the AAA+ activity. The goal of this project is to determine the three dimensional structure of different functional AAA+ assemblies in order to understand the common underlying mechanism of action of AAA+ proteins and its regulation by accessory factors. Using single particle cryo electron microscopy the functional states of (i) heat shock protein (Hsp) 100 variants with varying sized domain insertions, (ii) proteasomal subcomplexes and (iii) hetero oligomeric peroxisomal ATPase assemblies will be explored.

• DFG Programme: Independent Junior Research Groups