1g31: Difference between revisions
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[[Image:1g31.jpg|left|200px]]<br /><applet load="1g31" size=" | [[Image:1g31.jpg|left|200px]]<br /><applet load="1g31" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1g31, resolution 2.30Å" /> | caption="1g31, resolution 2.30Å" /> | ||
'''GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4'''<br /> | '''GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1G31 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t2 Enterobacteria phage t2] with PO4 and K as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=ML:The Mobile Loop (See Reference 1) Mediates Binding To Gr ...'>ML</scene>. Full crystallographic information is available from [http:// | 1G31 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t2 Enterobacteria phage t2] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=K:'>K</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=ML:The+Mobile+Loop+(See+Reference+1)+Mediates+Binding+To+Gr+...'>ML</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G31 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: in vivo protein folding]] | [[Category: in vivo protein folding]] | ||
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Revision as of 10:40, 3 February 2008
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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 with and as ligands. Known structural/functional Site: . 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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