(A) Overview of the oligomeric ClpC resting state 3D map coloured by subunits. (B) ClpC density map coloured by domains. Head-to-head interactions between MDs (green) of each helical assembly are key contacts stabilizing the ClpC resting state. ClpC domain organization is given, including an N-terminal domain (NT, yellow), AAA-1 large subdomain (L-AAA1, red), coiled-coil M-domain (MD, green), AAA-1 small subdomain (S, orange), AAA-2 large subdomain (L-AAA2, blue) and AAA-2 small subdomain (S, cyan). (C) Details of fitting for each ClpC subdomain. The small inset shows the positions relative to the whole molecule. (D) Zoomed view into MD-MD contacts highlighting conserved MD residues involved in interactions. The small inset shows the positions relative to the whole molecule. (E) Structure of the ClpC-MecA complex. Fitted atomic model coloured by ClpC domains as in b and MecA C-terminal domains (purple). Density for MecA N-terminal domains is indicated.