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Structural and functional analysis of the major AAA+ protease MecA/ClpC/ClpP from Staphylococcus aureus - 11 October 2022

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Speaker Dr Marta Carroni, Cell and Molecular Imaging Platform Director and Head of Unit, SciLifeLab CryoEM Facility, Department of Biochemistry & Biophysics, Stockholm University, Sweden

Title Structural and functional analysis of the major AAA+ protease MecA/ClpC/ClpP from Staphylococcus aureus

Host Julien Bergeron and James Torpey

 

Abstract The ClpC/ClpP AAA+ protease is a central component of bacterial protein quality control systems and play crucial roles for bacterial physiology, virulence and stress resistance. It is composed of the hexameric ATPase component ClpC and the barrel-shaped heptameric peptidase ClpP. ATP hydrolysis by ClpC fuels substrate unfolding and threading into associated ClpP for degradation. ClpC requires cooperation with specific adapter proteins such as MecA, which transfer substrates and strongly increase ClpC ATPase activity. ClpC and ClpP have been identified as antibacterial drug target underlining their crucial relevance for pathogenicity.

 

We determined the cryo EM structure of the MecA/ClpC/ClpP complex from the major pathogen Staphylococcus aureus. Combining structural analysis of the regions at the interface between the complex components and mutations functional studies, we describe the allosteric reciprocal regulation between the ATPase ClpC and the peptidase ClpP.


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