1G31

GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4

1G31 の概要

• エントリーDOI: 10.2210/pdb1g31/pdb
• 分子名称: GP31, PHOSPHATE ION, POTASSIUM ION, ... (4 entities in total)
• 機能のキーワード: chaperone, co-chaperonin, groes, in vivo protein folding, bacteriophage t4
• 由来する生物種: Enterobacteria phage T4
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 86878.52

構造登録者

Hunt, J.F.,Van Der Vies, S.M.,Henry, L.,Deisenhofer, J. (登録日: 1998-03-27, 公開日: 1998-08-26, 最終更新日: 2024-04-03)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.3 Å)