1g31

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[[Image:1g31.jpg|left|200px]]
[[Image:1g31.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1g31 |SIZE=350|CAPTION= <scene name='initialview01'>1g31</scene>, resolution 2.30&Aring;
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The line below this paragraph, containing "STRUCTURE_1g31", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=ML:The+Mobile+Loop+(See+Reference+1)+Mediates+Binding+To+Gr+...'>ML</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= 31 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 Enterobacteria phage T4])
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-->
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|DOMAIN=
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{{STRUCTURE_1g31| PDB=1g31 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g31 OCA], [http://www.ebi.ac.uk/pdbsum/1g31 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g31 RCSB]</span>
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}}
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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.]]
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[[Category: bacteriophage t4]]
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[[Category: Bacteriophage t4]]
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[[Category: chaperone]]
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[[Category: Chaperone]]
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[[Category: co-chaperonin]]
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[[Category: Co-chaperonin]]
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[[Category: roe]]
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[[Category: Roe]]
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[[Category: in vivo protein folding]]
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[[Category: In vivo protein folding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:04:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:35:34 2008''
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Revision as of 14:04, 2 May 2008

Image:1g31.jpg

Template:STRUCTURE 1g31

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 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 Fri May 2 17:04:41 2008

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