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-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL chaperonin.
Journal, issue, pages	Cell, Vol. 149, Issue 1, Page 113-123, Year 2012
Publish date	Mar 30, 2012
Authors	Daniel K Clare / Daven Vasishtan / Scott Stagg / Joel Quispe / George W Farr / Maya Topf / Arthur L Horwich / Helen R Saibil /
PubMed Abstract	The chaperonin GroEL assists the folding of nascent or stress-denatured polypeptides by actions of binding and encapsulation. ATP binding initiates a series of conformational changes triggering the ...The chaperonin GroEL assists the folding of nascent or stress-denatured polypeptides by actions of binding and encapsulation. ATP binding initiates a series of conformational changes triggering the association of the cochaperonin GroES, followed by further large movements that eject the substrate polypeptide from hydrophobic binding sites into a GroES-capped, hydrophilic folding chamber. We used cryo-electron microscopy, statistical analysis, and flexible fitting to resolve a set of distinct GroEL-ATP conformations that can be ordered into a trajectory of domain rotation and elevation. The initial conformations are likely to be the ones that capture polypeptide substrate. Then the binding domains extend radially to separate from each other but maintain their binding surfaces facing the cavity, potentially exerting mechanical force upon kinetically trapped, misfolded substrates. The extended conformation also provides a potential docking site for GroES, to trigger the final, 100° domain rotation constituting the "power stroke" that ejects substrate into the folding chamber.
External links	Cell / PubMed:22445172 / PubMed Central
Methods	EM (single particle)
Resolution	7.0 - 8.5 Å
Structure data	EMDB-1997: ATP-triggered molecular mechanics of the chaperonin GroEL Method: EM (single particle) / Resolution: 7.0 Å 1998 4aaq EMDB-1998, PDB-4aaq: ATP-triggered molecular mechanics of the chaperonin GroEL Method: EM (single particle) / Resolution: 8.0 Å 1999 4aar EMDB-1999, PDB-4aar: ATP-triggered molecular mechanics of the chaperonin GroEL Method: EM (single particle) / Resolution: 8.0 Å 2000 4aas EMDB-2000, PDB-4aas: ATP-triggered molecular mechanics of the chaperonin GroEL Method: EM (single particle) / Resolution: 8.5 Å 2001 4aau EMDB-2001, PDB-4aau: ATP-triggered molecular mechanics of the chaperonin GroEL Method: EM (single particle) / Resolution: 8.5 Å 2002 4ab2 EMDB-2002, PDB-4ab2: ATP-triggered molecular mechanics of the chaperonin GroEL Method: EM (single particle) / Resolution: 8.5 Å 2003 4ab3 EMDB-2003, PDB-4ab3: ATP-triggered molecular mechanics of the chaperonin GroEL Method: EM (single particle) / Resolution: 8.5 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM / Adenosine triphosphate ChemComp-PO4: PHOSPHATE ION / Phosphate ChemComp-MG*: Unknown entry
Source	escherichia coli (E. coli) synthetic construct (others)
Keywords	CHAPERONE