2C7D
Fitted coordinates for GroEL-ADP7-GroES Cryo-EM complex (EMD-1181)
Summary for 2C7D
| Entry DOI | 10.2210/pdb2c7d/pdb |
| Related | 1AON 1DK7 1DKD 1EGS 1FY9 1FYA 1GR5 1GR6 1GRL 1GRU 1J4Z 1JON 1KID 1KP8 1KPO 1LA1 1MNF 1OEL 1PCQ 1PF9 1SS8 1SVT 1SX3 1SX4 1XCK 2C7C 2C7E |
| EMDB information | 1181 |
| Descriptor | 60 KDA CHAPERONIN, 10 KDA CHAPERONIN MOLECULE: GROES, PROTEIN CPN10, GROES PROTEIN (2 entities in total) |
| Functional Keywords | atp-binding, chaperone, atomic structure fitting, cell cycle, cell division, chaperonin, nucleotide-binding, phosphorylation |
| Biological source | ESCHERICHIA COLI More |
| Total number of polymer chains | 21 |
| Total formula weight | 874453.62 |
| Authors | Ranson, N.A.,Clare, D.K.,Farr, G.W.,Houldershaw, D.,Horwich, A.L.,Saibil, H.R. (deposition date: 2005-11-22, release date: 2006-01-25, Last modification date: 2024-05-08) |
| Primary citation | Ranson, N.A.,Clare, D.K.,Farr, G.W.,Houldershaw, D.,Horwich, A.L.,Saibil, H.R. Allosteric Signalling of ATP Hydrolysis in Groel-Groes Complexes. Nat.Struct.Mol.Biol., 13:147-, 2006 Cited by PubMed Abstract: The double-ring chaperonin GroEL and its lid-like cochaperonin GroES form asymmetric complexes that, in the ATP-bound state, mediate productive folding in a hydrophilic, GroES-encapsulated chamber, the so-called cis cavity. Upon ATP hydrolysis within the cis ring, the asymmetric complex becomes able to accept non-native polypeptides and ATP in the open, trans ring. Here we have examined the structural basis for this allosteric switch in activity by cryo-EM and single-particle image processing. ATP hydrolysis does not change the conformation of the cis ring, but its effects are transmitted through an inter-ring contact and cause domain rotations in the mobile trans ring. These rigid-body movements in the trans ring lead to disruption of its intra-ring contacts, expansion of the entire ring and opening of both the nucleotide pocket and the substrate-binding domains, admitting ATP and new substrate protein. PubMed: 16429154DOI: 10.1038/NSMB1046 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (8.7 Å) |
Structure validation
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