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Structure paper

TitleClpC and ClpP act as reciprocal allosteric activators to form a highly efficient AAA+ protease
Journal, issue, pagesTo Be Published
Publish dateAug 16, 2024 (structure data deposition date)
AuthorsAzinas S / Wallden K / Katikaridis P / Schahl A / Mogk A / Carroni M
External linksSearch PubMed
MethodsEM (single particle)
Resolution3.0 - 3.5 Å
Structure data

51367

9gi1

EMDB-51367, PDB-9gi1:
Structure of the S.aureus MecA/ClpC/ClpP degradation system
Method: EM (single particle) / Resolution: 3.0 Å

51498

9goq

EMDB-51498, PDB-9goq:
Structure of the S.aureus MecA protein, in complex with ClpC
Method: EM (single particle) / Resolution: 3.5 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)
  • escherichia coli (E. coli)
  • staphylococcus (bacteria)
KeywordsCHAPERONE / protein-quality control / AAA+ unfoldases / peptidases / adaptor proteins / proteolysis / AAA+ adaptor protein / S.aureus

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