1g31: Difference between revisions
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==GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4== | |||
<StructureSection load='1g31' size='340' side='right'caption='[[1g31]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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> | |||
== | <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> | ||
[[1g31]] is a 7 chain structure with sequence from [ | </table> | ||
== 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 == | ||
[[ | [[Image:Consurf_key_small.gif|200px|right]] | ||
[[ | Check<jmol> | ||
[[ | <jmolCheckbox> | ||
[[ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g3/1g31_consurf.spt"</scriptWhenChecked> | ||
[[Category: | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
[[Category: | <text>to colour the structure by Evolutionary Conservation</text> | ||
[[Category: | </jmolCheckbox> | ||
[[Category: | </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: | <div style="clear:both"></div> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[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
FunctionVG31_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. |
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