1GRU
SOLUTION STRUCTURE OF GROES-ADP7-GROEL-ATP7 COMPLEX BY CRYO-EM
Summary for 1GRU
| Entry DOI | 10.2210/pdb1gru/pdb |
| Related | 1AON 1DER 1EGS 1FY9 1FYA 1GR5 1GR6 1GRL 1JON 1KID 1OEL |
| EMDB information | 1046 |
| Descriptor | GROEL, GROES (2 entities in total) |
| Functional Keywords | chaperone, chaperonin, hsp60, groel-groes, molecular chaperone, adp |
| Biological source | ESCHERICHIA COLI More |
| Total number of polymer chains | 21 |
| Total formula weight | 874453.62 |
| Authors | Ranson, N.A.,Farr, G.W.,Roseman, A.M.,Gowen, B.,Fenton, W.A.,Horwich, A.L.,Saibil, H.R. (deposition date: 2001-12-16, 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 Cited by 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: 11779463DOI: 10.1016/S0092-8674(01)00617-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (12.5 Å) |
Structure validation
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