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TitleStructure of the central Staphylococcus aureus AAA+ protease MecA/ClpC/ClpP.
Journal, issue, pagesCommun Biol, Vol. 8, Issue 1, Page 1467, Year 2025
Publish dateOct 14, 2025
AuthorsStavros Azinas / Karin Wallden / Panagiotis Katikaridis / Timo Jenne / Adrien Schahl / Axel Mogk / Marta Carroni /
PubMed AbstractBacterial AAA+ proteases are composed of a AAA+ partner (e.g., ClpC) and an associated peptidase (e.g., ClpP). They represent ATP-fuelled and self-compartmentalized proteolytic machines that are ...Bacterial AAA+ proteases are composed of a AAA+ partner (e.g., ClpC) and an associated peptidase (e.g., ClpP). They represent ATP-fuelled and self-compartmentalized proteolytic machines that are crucial for stress resistance and virulence. ClpC requires cooperation with adaptor proteins such as MecA for activation and complex formation with ClpP. Here, we present the cryo-EM structure of the MecA/ClpC/ClpP complex from the major pathogen Staphylococcus aureus. MecA forms a dynamic crown on top of the ClpC/ClpP complex with its substrate-binding domain positioned near the ClpC pore site, likely facilitating substrate transfer. ClpC/ClpP complex formation involves ClpC P-loops and ClpP N-terminal β-hairpins, which insert into the central ClpC threading channel and contact sites next to the ClpC ATPase center. ClpC and ClpP interactions are asymmetric and dictated by the activity states of ClpC ATPase subunits. ClpP binding increases ClpC ATPase and threading activities in a β-hairpin dependent manner, illuminating an allosteric pathway in the cooperation of ATPase and peptidase components in bacterial AAA+ proteases.
External linksCommun Biol / PubMed:41087538 / PubMed Central
MethodsEM (single particle)
Resolution2.68 - 3.0 Å
Structure data

53538

9r2s

EMDB-53538, PDB-9r2s:
Structure of the S.aureus ClpP degradation chamber in the context of the MecA/ClpC/CLpC complex
Method: EM (single particle) / Resolution: 2.68 Å

53879

9rai

EMDB-53879, PDB-9rai:
Structure of the S.aureus MecA/ClpC/ClpP degradation system
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

Source
  • staphylococcus aureus (bacteria)
KeywordsCHAPERONE / protein-quality control / AAA+ unfoldases / peptidase / adaptor proteins / peptidases

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