1GR5

Solution Structure of apo GroEL by Cryo-Electron microscopy

Summary for 1GR5

• Entry DOI: 10.2210/pdb1gr5/pdb
• Related: 1AON 1DER 1FY9 1FYA 1GRL 1GRU 1JON 1KID 1OEL 2C7E
• EMDB information: 1042 1047
• Descriptor: 60 KDA CHAPERONIN (1 entity in total)
• Functional Keywords: chaperone
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 14
• Total formula weight: 800637.74

Authors

Ranson, N.A.,Farr, G.W.,Roseman, A.M.,Gowen, B.,Fenton, W.A.,Horwich, A.L.,Saibil, H.R. (deposition date: 2001-12-14, release date: 2002-01-28, Last modification date: 2024-05-08)

Primary citation

Ranson, N.A.,Farr, G.W.,Roseman, A.M.,Gowen, B.,Fenton, W.A.,Horwich, A.L.,Saibil, H.R.
ATP-Bound States of Groel Captured by Cryo-Electron Microscopy.
Cell(Cambridge,Mass.), 107:869-, 2001

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 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.

PubMed: 11779463
DOI: 10.1016/S0092-8674(01)00617-1

Experimental method

ELECTRON MICROSCOPY (7.9 Å)