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1g31

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{{STRUCTURE_1g31| PDB=1g31 | SCENE= }}
{{STRUCTURE_1g31| PDB=1g31 | SCENE= }}
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'''GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4'''
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===GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_9244309}}
==About this Structure==
==About this Structure==
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[[Category: Roe]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:20:26 2008''

Revision as of 01:20, 1 July 2008

Image:1g31.png

Template:STRUCTURE 1g31

GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4

Template:ABSTRACT PUBMED 9244309

About this Structure

1G31 is a Single protein structure of sequence from Enterobacteria phage t4. 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 Tue Jul 1 04:20:26 2008

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