STRUCTURAL ADAPTATIONS IN THE SPECIALIZED BACTERIOPHAGE-T4 CO-CHAPERONIN GP31 EXPAND THE SIZE OF THE ANFINSEN CAGE

The Gp31 protein from bacteriophage T4 functionally substitutes for th e 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 ca nnot be satisfied by GroES. The 2.3 Angstrom crystal structure of Gp31 shows that its tertiary and quaternary structures are similar to thos e of GroES despite the existence of only 14% sequence identity between the two proteins. However, Gp31 shows a series of structural adaptati ons which will increase the size and the hydrophilicity of the ''Anfin sen cage,'' the enclosed cavity within the GroEL/GroES complex that is the location of the chaperonin-assisted protein folding reaction.