2cgt

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[[Image:2cgt.png|left|200px]]
 
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{{STRUCTURE_2cgt| PDB=2cgt | SCENE= }}
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==GROEL-ADP-gp31 COMPLEX==
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<SX load='2cgt' size='340' side='right' viewer='molstar' caption='[[2cgt]], [[Resolution|resolution]] 8.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2cgt]] is a 21 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [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=2CGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CGT FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8.2&#8491;</td></tr>
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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=2cgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cgt OCA], [https://pdbe.org/2cgt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cgt RCSB], [https://www.ebi.ac.uk/pdbsum/2cgt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cgt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CH60_ECOLI CH60_ECOLI] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.[HAMAP-Rule:MF_00600] Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.[HAMAP-Rule:MF_00600]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cg/2cgt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2cgt ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Bacteriophage T4 produces a GroES analogue, gp31, which cooperates with the Escherichia coli GroEL to fold its major coat protein gp23. We have used cryo-electron microscopy and image processing to obtain three-dimensional structures of the E.coli chaperonin GroEL complexed with gp31, in the presence of both ATP and ADP. The GroEL-gp31-ADP map has a resolution of 8.2 A, which allows accurate fitting of the GroEL and gp31 crystal structures. Comparison of this fitted structure with that of the GroEL-GroES-ADP structure previously determined by cryo-electron microscopy shows that the folding cage is expanded. The enlarged volume for folding is consistent with the size of the bacteriophage coat protein gp23, which is the major substrate of GroEL-gp31 chaperonin complex. At 56 kDa, gp23 is close to the maximum size limit of a polypeptide that is thought to fit inside the GroEL-GroES folding cage.
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===GROEL-ADP-GP31 COMPLEX===
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An expanded protein folding cage in the GroEL-gp31 complex.,Clare DK, Bakkes PJ, van Heerikhuizen H, van der Vies SM, Saibil HR J Mol Biol. 2006 May 5;358(3):905-11. Epub 2006 Mar 6. PMID:16549073<ref>PMID:16549073</ref>
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{{ABSTRACT_PUBMED_16549073}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 2cgt" style="background-color:#fffaf0;"></div>
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[[2cgt]] is a 21 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CGT OCA].
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==See Also==
==See Also==
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*[[Chaperonin|Chaperonin]]
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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*[[Heat Shock Proteins|Heat Shock Proteins]]
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:016549073</ref><references group="xtra"/>
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</SX>
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[[Category: Enterobacteria phage t4]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Bakkes, P J.]]
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[[Category: Escherichia virus T4]]
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[[Category: Clare, D K.]]
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[[Category: Large Structures]]
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[[Category: Heerikhuizen, H Van.]]
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[[Category: Bakkes PJ]]
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[[Category: Saibil, H R.]]
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[[Category: Clare DK]]
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[[Category: Vies, S M.Van Der.]]
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[[Category: Saibil HR]]
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[[Category: Capsid assembly]]
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[[Category: Van Heerikhuizen H]]
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[[Category: Cell cycle]]
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[[Category: Van der Vies SM]]
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[[Category: Cell division]]
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[[Category: Chaperone]]
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[[Category: Chaperonin]]
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[[Category: Early protein]]
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[[Category: Gp31]]
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[[Category: Groel]]
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Current revision

GROEL-ADP-gp31 COMPLEX

2cgt, resolution 8.20Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

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