1G31

GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4

Summary for 1G31

• Entry DOI: 10.2210/pdb1g31/pdb
• Descriptor: GP31, PHOSPHATE ION, POTASSIUM ION, ... (4 entities in total)
• Functional Keywords: chaperone, co-chaperonin, groes, in vivo protein folding, bacteriophage t4
• Biological source: Enterobacteria phage T4
• Total number of polymer chains: 7
• Total formula weight: 86878.52

Authors

Hunt, J.F.,Van Der Vies, S.M.,Henry, L.,Deisenhofer, J. (deposition date: 1998-03-27, release date: 1998-08-26, Last modification date: 2024-04-03)

Primary citation

Hunt, J.F.,van der Vies, S.M.,Henry, L.,Deisenhofer, J.
Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage.
Cell(Cambridge,Mass.), 90:361-371, 1997

PubMed Abstract: The Gp31 protein from bacteriophage T4 functionally substitutes for the bacterial co-chaperonin GroES in assisted protein folding reactions both in vitro and in vivo. But Gp31 is required for the folding and/or assembly of the T4 major capsid protein Gp23, and this requirement cannot be satisfied by GroES. The 2.3 A crystal structure of Gp31 shows that its tertiary and quaternary structures are similar to those of GroES despite the existence of only 14% sequence identity between the two proteins. However, Gp31 shows a series of structural adaptations which will increase the size and the hydrophilicity of the "Anfinsen cage," the enclosed cavity within the GroEL/GroES complex that is the location of the chaperonin-assisted protein folding reaction.

PubMed: 9244309
DOI: 10.1016/S0092-8674(00)80343-8

Experimental method

X-RAY DIFFRACTION (2.3 Å)