1g31: Difference between revisions
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[[Image:1g31.jpg|left|200px]] | [[Image:1g31.jpg|left|200px]] | ||
'''GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4''' | {{Structure | ||
|PDB= 1g31 |SIZE=350|CAPTION= <scene name='initialview01'>1g31</scene>, resolution 2.30Å | |||
|SITE= <scene name='pdbsite=ML:The+Mobile+Loop+(See+Reference+1)+Mediates+Binding+To+Gr+...'>ML</scene> | |||
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=K:POTASSIUM ION'>K</scene> | |||
|ACTIVITY= | |||
|GENE= 31 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10664 Enterobacteria phage T2]) | |||
}} | |||
'''GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1G31 is a [ | 1G31 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t2 Enterobacteria phage t2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G31 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9244309 9244309] | ||
[[Category: Enterobacteria phage t2]] | [[Category: Enterobacteria phage t2]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: chaperone]] | [[Category: chaperone]] | ||
[[Category: co-chaperonin]] | [[Category: co-chaperonin]] | ||
[[Category: | [[Category: roe]] | ||
[[Category: in vivo protein folding]] | [[Category: in vivo protein folding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:17:32 2008'' | ||
Revision as of 12:17, 20 March 2008
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| , resolution 2.30Å | |||||||
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| Sites: | |||||||
| Ligands: | and | ||||||
| Gene: | 31 (Enterobacteria phage T2) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 t2. 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
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