2cgt
From Proteopedia
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(New page: 200px<br /><applet load="2cgt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cgt" /> '''GROEL-ADP-GP31 COMPLEX'''<br /> ==Overview=...) |
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| - | [[Image:2cgt.gif|left|200px]]<br /><applet load="2cgt" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2cgt" /> | ||
| - | '''GROEL-ADP-GP31 COMPLEX'''<br /> | ||
| - | == | + | ==GROEL-ADP-gp31 COMPLEX== |
| - | Bacteriophage T4 produces a GroES analogue, gp31, which cooperates with | + | <SX load='2cgt' size='340' side='right' viewer='molstar' caption='[[2cgt]], [[Resolution|resolution]] 8.20Å' scene=''> |
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8.2Å</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=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> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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] | ||
| + | == 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/cg/2cgt_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2cgt" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Escherichia virus T4]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bakkes PJ]] | ||
| + | [[Category: Clare DK]] | ||
| + | [[Category: Saibil HR]] | ||
| + | [[Category: Van Heerikhuizen H]] | ||
| + | [[Category: Van der Vies SM]] | ||
Current revision
GROEL-ADP-gp31 COMPLEX
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