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|1g31, resolution 2.30Å ()|
|Gene:||31 (Enterobacteria phage T4)|
GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4
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.
Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage., Hunt JF, van der Vies SM, Henry L, Deisenhofer J, Cell. 1997 Jul 25;90(2):361-71. PMID:9244309
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Hunt JF, van der Vies SM, Henry L, Deisenhofer J. Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage. Cell. 1997 Jul 25;90(2):361-71. PMID:9244309
- Numoto N, Kita A, Miki K. Crystal structure of the Co-chaperonin Cpn10 from Thermus thermophilus HB8. Proteins. 2005 Feb 1;58(2):498-500. PMID:15558581 doi:10.1002/prot.20317