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1g31

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[[Image:1g31.jpg|left|200px]]<br /><applet load="1g31" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1g31, resolution 2.30&Aring;" />
 
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'''GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4'''<br />
 
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==Overview==
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==GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4==
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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.
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<StructureSection load='1g31' size='340' side='right'caption='[[1g31]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<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>
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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].
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</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>
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<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>
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==Reference==
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<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>
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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]
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</table>
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[[Category: Enterobacteria phage t2]]
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== Function ==
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[[Category: Single protein]]
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[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.
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[[Category: Deisenhofer, J.]]
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== Evolutionary Conservation ==
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[[Category: Henry, L.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Hunt, J.F.]]
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Check<jmol>
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[[Category: Vies, S.M.Van.Der.]]
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<jmolCheckbox>
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[[Category: K]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g3/1g31_consurf.spt"</scriptWhenChecked>
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[[Category: PO4]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: bacteriophage t4]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: chaperone]]
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</jmolCheckbox>
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[[Category: co-chaperonin]]
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</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].
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[[Category: groes]]
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<div style="clear:both"></div>
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[[Category: in vivo protein folding]]
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__TOC__
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</StructureSection>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:40:18 2008''
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[[Category: Escherichia virus T4]]
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[[Category: Large Structures]]
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[[Category: Deisenhofer J]]
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[[Category: Henry L]]
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[[Category: Hunt JF]]
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[[Category: Van Der Vies SM]]

Current revision

GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4

PDB ID 1g31

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