1g31: Difference between revisions

Revision as of 13:45, 21 February 2008

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

Page seeded by OCA on Thu Feb 21 12:45:46 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 15: / Line 15: @@
 [[Category: Deisenhofer, J.]]
 [[Category: Henry, L.]]
-[[Category: Hunt, J.F.]]
+[[Category: Hunt, J F.]]
-[[Category: Vies, S.M.Van.Der.]]
+[[Category: Vies, S M.Van Der.]]
 [[Category: K]]
 [[Category: PO4]]
@@ Line 25: / Line 25: @@
 [[Category: in vivo protein folding]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:40:18 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:45:46 2008''