Skip to main content

Active Structure of ClpX Bound to SsrA substrate


EMSL Project ID
50690

Abstract

AAA+ ATPases are involved in myriad cellular functions, including cell membrane reformation, chromatin remodeling, protein degradation and quality control. Our lab is investigating the mechanism, substrate recognition and partner interactions of several AAA+ ATPases. Human Vps4 drives membrane fission by remodeling and dissembling ESCRT-III filaments during HIV viral budding. Our work on Vps4 proposes a conserved mechanism amongst these AAA+ ATPases whereby pore loops at the center of the hexamers interact with peptide substrates and pull them through the pore using a ‘conveyor belt’ model where four ATP-bound subunits “hold” the peptide while the 5th and 6th subunits hydrolyze ATP and translocate from one end of the complex pore to the other in order to walk the peptide through the pore (Monroe, 2017; Han, 2018). Our extended studies will expand to other enzymes, explore substrate recognition, coupling proteins and co-factors. In particular, this proposal seeks to explore the true mechanism of ClpX through the evaluation of a substrate bound complex.

Project Details

Start Date
2019-03-15
End Date
2019-10-15
Status
Closed

Team

Principal Investigator

Christopher Hill
Institution
University of Utah

Co-Investigator(s)

Heidi Schubert
Institution
University of Utah

Team Members

Nancy Meyer
Institution
Oregon Health & Science University