1g31

GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4

Structural highlights 1g31 is a 7 chain structure with sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , Gene: 31 (Enterobacteria phage T4) Resources: FirstGlance, OCA, RCSB, PDBsum Function [VG31_BPT4] Essential for proper capsid assembly. In absence of Gp31 the major capsid protein (Gp23) assembles into 'lumps'. Acts as a co-chaperonin with the host groEL protein. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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.

spinqualitylabelsall models 1g31, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image