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[[Image:1g31.jpg|left|200px]]<br /><applet load="1g31" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1g31, resolution 2.30&Aring;" />
'''GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4'''<br />


==Overview==
==GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4==
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.
<StructureSection load='1g31' size='340' side='right'caption='[[1g31]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<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>
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G31 OCA].  
</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>
 
<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>
==Reference==
<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>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9244309 9244309]
</table>
[[Category: Enterobacteria phage t2]]
== Function ==
[[Category: Single protein]]
[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.
[[Category: Deisenhofer, J.]]
== Evolutionary Conservation ==
[[Category: Henry, L.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Hunt, J.F.]]
Check<jmol>
[[Category: Vies, S.M.Van.Der.]]
  <jmolCheckbox>
[[Category: K]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g3/1g31_consurf.spt"</scriptWhenChecked>
[[Category: PO4]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: bacteriophage t4]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: chaperone]]
  </jmolCheckbox>
[[Category: co-chaperonin]]
</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].
[[Category: groes]]
<div style="clear:both"></div>
[[Category: in vivo protein folding]]
__TOC__
 
</StructureSection>
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:18:47 2007''
[[Category: Escherichia virus T4]]
[[Category: Large Structures]]
[[Category: Deisenhofer J]]
[[Category: Henry L]]
[[Category: Hunt JF]]
[[Category: Van Der Vies SM]]

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

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