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1g31
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The Gp31 protein from bacteriophage T4 functionally substitutes for the | + | 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 Structure== | ==About this Structure== | ||
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[[Category: Deisenhofer, J.]] | [[Category: Deisenhofer, J.]] | ||
[[Category: Henry, L.]] | [[Category: Henry, L.]] | ||
| - | [[Category: Hunt, J | + | [[Category: Hunt, J F.]] |
| - | [[Category: Vies, S | + | [[Category: Vies, S M.Van Der.]] |
[[Category: K]] | [[Category: K]] | ||
[[Category: PO4]] | [[Category: PO4]] | ||
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[[Category: in vivo protein folding]] | [[Category: in vivo protein folding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:45:46 2008'' |
Revision as of 10:45, 21 February 2008
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GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4
Overview
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 Structure
1G31 is a Single protein structure of sequence from Enterobacteria phage t2 with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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 Thu Feb 21 12:45:46 2008
