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TitleATP-bound states of GroEL captured by cryo-electron microscopy.
Journal, issue, pagesCell, Vol. 107, Issue 7, Page 869-879, Year 2001
Publish dateDec 28, 2001
AuthorsN A Ranson / G W Farr / A M Roseman / B Gowen / W A Fenton / A L Horwich / H R Saibil /
PubMed AbstractThe chaperonin GroEL drives its protein-folding cycle by cooperatively binding ATP to one of its two rings, priming that ring to become folding-active upon GroES binding, while simultaneously ...The chaperonin GroEL drives its protein-folding cycle by cooperatively binding ATP to one of its two rings, priming that ring to become folding-active upon GroES binding, while simultaneously discharging the previous folding chamber from the opposite ring. The GroEL-ATP structure, determined by cryo-EM and atomic structure fitting, shows that the intermediate domains rotate downward, switching their intersubunit salt bridge contacts from substrate binding to ATP binding domains. These observations, together with the effects of ATP binding to a GroEL-GroES-ADP complex, suggest structural models for the ATP-induced reduction in affinity for polypeptide and for cooperativity. The model for cooperativity, based on switching of intersubunit salt bridge interactions around the GroEL ring, may provide general insight into cooperativity in other ring complexes and molecular machines.
External linksCell / PubMed:11779463
MethodsEM (single particle)
Resolution7.9 - 23.5 Å
Structure data

EMDB-1042: ATP-bound states of GroEL captured by cryo-electron microscopy.
PDB-1gr5: Solution Structure of apo GroEL by Cryo-Electron microscopy
Method: EM (single particle) / Resolution: 10.3 Å

EMDB-1046: ATP-bound states of GroEL captured by cryo-electron microscopy.
PDB-1gru: SOLUTION STRUCTURE OF GROES-ADP7-GROEL-ATP7 COMPLEX BY CRYO-EM
Method: EM (single particle) / Resolution: 23.5 Å

EMDB-1047: ATP-bound states of GroEL captured by cryo-electron microscopy.
PDB-2c7e: REVISED ATOMIC STRUCTURE FITTING INTO A GROEL(D398A)-ATP7 CRYO-EM MAP (EMD 1047)
Method: EM (single particle) / Resolution: 14.9 Å

Chemicals

ChemComp-K:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsCHAPERONE / CHAPERONIN / HSP60 / GROEL-GROES / MOLECULAR CHAPERONE / ADP / CELL CYCLE / ATP-BINDING / D398A / HP60 CLASS / CELL DIVISION / NUCLEOTIDE-BINDING / PHOSPHORYLATION

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