1g31
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(New page: 200px<br /> <applet load="1g31" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g31, resolution 2.30Å" /> '''GP31 CO-CHAPERONIN ...)
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Revision as of 19:28, 29 October 2007
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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 [Bacteriophage t4] with PO4 and K as [ligands]. 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 Mon Oct 29 21:32:49 2007
