Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	ATP-bound states of GroEL captured by cryo-electron microscopy.
Journal, issue, pages	Cell, Vol. 107, Issue 7, Page 869-879, Year 2001
Publish date	Dec 28, 2001
Authors	N A Ranson / G W Farr / A M Roseman / B Gowen / W A Fenton / A L Horwich / H R Saibil /
PubMed Abstract	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 ...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 links	Cell / PubMed:11779463
Methods	EM (single particle)
Resolution	7.9 - 23.5 Å
Structure data	1042 1gr5 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 1046 1gru 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 1047 2c7e 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 moleculeYM ChemComp-HOH*: WATER
Source	escherichia coli (E. coli)
Keywords	CHAPERONE / CHAPERONIN / HSP60 / GROEL-GROES / MOLECULAR CHAPERONE / ADP / CELL CYCLE / ATP-BINDING / D398A / HP60 CLASS / CELL DIVISION / NUCLEOTIDE-BINDING / PHOSPHORYLATION