1g31: Difference between revisions

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-[[Image:1g31.gif|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>
-G31 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]]. Structure known Active Site: ML. 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 Oct 30 14:06:06 2007''
+[[Category: Escherichia virus T4]]
+[[Category: Large Structures]]
+[[Category: Deisenhofer J]]
+[[Category: Henry L]]
+[[Category: Hunt JF]]
+[[Category: Van Der Vies SM]]