Projects

Our aim is to solve the conformational dynamics of AAA+ assemblies at the highest possible resolution using single particle cryo EM. Ultimately we record molecular snapshots of the ATPase complexes in order to correlate functional states with structural data. We are particularly interested in understanding how the AAA+ motor function is regulated by neighboring AAA+ modules in the active oligomer and by accessory factors in the complex. Furthermore, we hope to indentify mechanisms that define specificity or are intrinsic to all AAA+ proteins.

The lab is working on a range of different ATPase assemblies. We investigate the location and interaction partners of the proteasomal 19S ATPases and want to gain insight into the movements of the 19S base on top of the proteolytic 20S chamber. Using several structural and biophysical methods we aim to characterise peroxisomal AAA+ assemblies consisting of mixed hexamers of peroxins Pex1 and Pex6. We also work on the structural characterisation of ATPase dependent aspects of the Type VI secretion system of bacterial pathogens and expect to provide greater insight into the structural and functional significance of the coild-coil insertion in Hsp100 proteins.

Further details will be available on this webpage in the near future.