1g31: Difference between revisions

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[[Image:1g31.jpg|left|200px]]
[[Image:1g31.jpg|left|200px]]


{{Structure
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|PDB= 1g31 |SIZE=350|CAPTION= <scene name='initialview01'>1g31</scene>, resolution 2.30&Aring;
The line below this paragraph, containing "STRUCTURE_1g31", creates the "Structure Box" on the page.
|SITE= <scene name='pdbsite=ML:The+Mobile+Loop+(See+Reference+1)+Mediates+Binding+To+Gr+...'>ML</scene>
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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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|ACTIVITY=
or leave the SCENE parameter empty for the default display.
|GENE= 31 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 Enterobacteria phage T4])
-->
|DOMAIN=
{{STRUCTURE_1g31| PDB=1g31  | SCENE= }}  
|RELATEDENTRY=
|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>
}}


'''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: bacteriophage t4]]
[[Category: Bacteriophage t4]]
[[Category: chaperone]]
[[Category: Chaperone]]
[[Category: co-chaperonin]]
[[Category: Co-chaperonin]]
[[Category: roe]]
[[Category: Roe]]
[[Category: in vivo protein folding]]
[[Category: In vivo protein folding]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:04:41 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:35:34 2008''

Revision as of 17:04, 2 May 2008

File:1g31.jpg

Template:STRUCTURE 1g31

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

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