2CGT
GROEL-ADP-gp31 COMPLEX
Summary for 2CGT
Entry DOI | 10.2210/pdb2cgt/pdb |
Related | 1AON 1DK7 1DKD 1FY9 1FYA 1G31 1GR5 1GRL 1GRU 1J4Z 1JON 1KID 1KP8 1KPO 1LA1 1MNF 1OEL 1PCQ 1PF9 1SS8 1SVT 1SX3 1SX4 1XCK 2C7C 2C7D 2C7E |
EMDB information | 1202 |
Descriptor | 60 KDA GROEL, CAPSID ASSEMBLY PROTEIN GP31 (2 entities in total) |
Functional Keywords | chaperonin, chaperone, cell cycle, cell division, capsid assembly, early protein |
Biological source | ESCHERICHIA COLI More |
Total number of polymer chains | 21 |
Total formula weight | 886291.05 |
Authors | Clare, D.K.,Bakkes, P.J.,van Heerikhuizen, H.,van der Vies, S.M.,Saibil, H.R. (deposition date: 2006-03-09, release date: 2006-03-29, Last modification date: 2024-05-08) |
Primary citation | Clare, D.K.,Bakkes, P.J.,Van Heerikhuizen, H.,Van Der Vies, S.M.,Saibil, H.R. An Expanded Protein Folding Cage in the Groel-Gp31 Complex. J.Mol.Biol., 358:905-, 2006 Cited by PubMed Abstract: Bacteriophage T4 produces a GroES analogue, gp31, which cooperates with the Escherichia coli GroEL to fold its major coat protein gp23. We have used cryo-electron microscopy and image processing to obtain three-dimensional structures of the E.coli chaperonin GroEL complexed with gp31, in the presence of both ATP and ADP. The GroEL-gp31-ADP map has a resolution of 8.2 A, which allows accurate fitting of the GroEL and gp31 crystal structures. Comparison of this fitted structure with that of the GroEL-GroES-ADP structure previously determined by cryo-electron microscopy shows that the folding cage is expanded. The enlarged volume for folding is consistent with the size of the bacteriophage coat protein gp23, which is the major substrate of GroEL-gp31 chaperonin complex. At 56 kDa, gp23 is close to the maximum size limit of a polypeptide that is thought to fit inside the GroEL-GroES folding cage. PubMed: 16549073DOI: 10.1016/J.JMB.2006.02.033 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (8.2 Å) |
Structure validation
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