1g31: Difference between revisions
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{{STRUCTURE_1g31| PDB=1g31 | SCENE= }} | |||
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'''GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4''' | '''GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4''' | ||
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[[Category: Hunt, J F.]] | [[Category: Hunt, J F.]] | ||
[[Category: Vies, S M.Van Der.]] | [[Category: Vies, S M.Van Der.]] | ||
[[Category: | [[Category: Bacteriophage t4]] | ||
[[Category: | [[Category: Chaperone]] | ||
[[Category: | [[Category: Co-chaperonin]] | ||
[[Category: | [[Category: Roe]] | ||
[[Category: | [[Category: In vivo protein folding]] | ||
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Revision as of 17:04, 2 May 2008
GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4
OverviewOverview
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.
About this StructureAbout this Structure
1G31 is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Fri May 2 17:04:41 2008