1g31: Difference between revisions

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


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==GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4==
The line below this paragraph, containing "STRUCTURE_1g31", creates the "Structure Box" on the page.
<StructureSection load='1g31' size='340' side='right'caption='[[1g31]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
{{STRUCTURE_1g31|  PDB=1g31  |  SCENE=  }}
<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>
 
</table>
===GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4===
== 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 ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g3/1g31_consurf.spt"</scriptWhenChecked>
{{ABSTRACT_PUBMED_9244309}}
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    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
1G31 is a 7 chains structure of sequences 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__
<ref group="xtra">PMID:9244309</ref><references group="xtra"/>
</StructureSection>
[[Category: Enterobacteria phage t4]]
[[Category: Escherichia virus T4]]
[[Category: Deisenhofer, J.]]
[[Category: Large Structures]]
[[Category: Henry, L.]]
[[Category: Deisenhofer J]]
[[Category: Hunt, J F.]]
[[Category: Henry L]]
[[Category: Vies, S M.Van Der.]]
[[Category: Hunt JF]]
[[Category: Bacteriophage t4]]
[[Category: Van Der Vies SM]]
[[Category: Chaperone]]
[[Category: Co-chaperonin]]
[[Category: Roe]]
[[Category: In vivo protein folding]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 11:41:13 2009''

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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