Summary:
BRUCE (BIRC6), a giant E3 ubiquitin ligase is a member of the Inhibitor of Apoptosis Protein (IAP) family of proteins that regulates programmed cell death amongst other processes. Mechanistic details of what BRUCE looks like or how BRUCE achieves these functions have been lacking. I will present our insights into the first complete structure of BRUCE alone and in complex with SMAC, an antagonist of BRUCE and other IAPs. Importantly, I will also present the first thorough biochemical characterisation of BRUCE revealing how it restricts caspase activities and how sub-nanomolar binding of SMAC to BRUCE antagonises BRUCEs ability to restrict caspase activity, paving the way for future studies on this most almighty of proteins.

Bio:

Paul is an MRC Career Development Fellow at the Department of Biochemistry, University of Oxford and established his laboratory in autumn 2018. Prior to this he spent seven years working with David Komander at the MRC Laboratory of Molecular Biology, Cambridge and in a former life worked with Igor Barsukov at the University of Liverpool and obtained his PhD from the University of Leicester under the supervision of Peter Moody.