1g31: Difference between revisions

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


{{Structure
==GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4==
|PDB= 1g31 |SIZE=350|CAPTION= <scene name='initialview01'>1g31</scene>, resolution 2.30&Aring;
<StructureSection load='1g31' size='340' side='right'caption='[[1g31]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
|SITE= <scene name='pdbsite=ML:The+Mobile+Loop+(See+Reference+1)+Mediates+Binding+To+Gr+...'>ML</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
<table><tr><td colspan='2'>[[1g31]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G31 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
|GENE= 31 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 Enterobacteria phage T4])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g31 OCA], [https://pdbe.org/1g31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g31 RCSB], [https://www.ebi.ac.uk/pdbsum/1g31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g31 ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|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>
== Function ==
}}
[https://www.uniprot.org/uniprot/VG31_BPT4 VG31_BPT4] Essential for proper capsid assembly. In absence of Gp31 the major capsid protein (Gp23) assembles into 'lumps'. Acts as a co-chaperonin with the host groEL protein.
 
== Evolutionary Conservation ==
'''GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g3/1g31_consurf.spt"</scriptWhenChecked>
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.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
1G31 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G31 OCA].  
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1g31 ConSurf].
 
<div style="clear:both"></div>
==Reference==
__TOC__
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]
</StructureSection>
[[Category: Enterobacteria phage t4]]
[[Category: Escherichia virus T4]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Deisenhofer, J.]]
[[Category: Deisenhofer J]]
[[Category: Henry, L.]]
[[Category: Henry L]]
[[Category: Hunt, J F.]]
[[Category: Hunt JF]]
[[Category: Vies, S M.Van Der.]]
[[Category: Van Der Vies SM]]
[[Category: bacteriophage t4]]
[[Category: chaperone]]
[[Category: co-chaperonin]]
[[Category: roe]]
[[Category: in vivo protein folding]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:35:34 2008''

Latest revision as of 10:22, 7 February 2024

GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4

Structural highlights

1g31 is a 7 chain structure with sequence from Escherichia virus T4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VG31_BPT4 Essential for proper capsid assembly. In absence of Gp31 the major capsid protein (Gp23) assembles into 'lumps'. Acts as a co-chaperonin with the host groEL protein.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1g31, resolution 2.30Å

Drag the structure with the mouse to rotate

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