2c7c

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(New page: 200px<br /><applet load="2c7c" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c7c" /> '''FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO...)
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[[Image:2c7c.gif|left|200px]]<br /><applet load="2c7c" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2c7c" />
 
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'''FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)'''<br />
 
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==Overview==
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==FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)==
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The double-ring chaperonin GroEL and its lid-like cochaperonin GroES form, asymmetric complexes that, in the ATP-bound state, mediate productive, folding in a hydrophilic, GroES-encapsulated chamber, the so-called cis, cavity. Upon ATP hydrolysis within the cis ring, the asymmetric complex, becomes able to accept non-native polypeptides and ATP in the open, trans, ring. Here we have examined the structural basis for this allosteric, switch in activity by cryo-EM and single-particle image processing. ATP, hydrolysis does not change the conformation of the cis ring, but its, effects are transmitted through an inter-ring contact and cause domain, rotations in the mobile trans ring. These rigid-body movements in the, trans ring lead to disruption of its intra-ring contacts, expansion of the, entire ring and opening of both the nucleotide pocket and the, substrate-binding domains, admitting ATP and new substrate protein.
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<SX load='2c7c' size='340' side='right' viewer='molstar' caption='[[2c7c]], [[Resolution|resolution]] 7.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2c7c]] is a 21 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C7C 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]] 7.7&#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=2c7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c7c OCA], [https://pdbe.org/2c7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c7c RCSB], [https://www.ebi.ac.uk/pdbsum/2c7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c7c 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/c7/2c7c_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=2c7c 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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The double-ring chaperonin GroEL and its lid-like cochaperonin GroES form asymmetric complexes that, in the ATP-bound state, mediate productive folding in a hydrophilic, GroES-encapsulated chamber, the so-called cis cavity. Upon ATP hydrolysis within the cis ring, the asymmetric complex becomes able to accept non-native polypeptides and ATP in the open, trans ring. Here we have examined the structural basis for this allosteric switch in activity by cryo-EM and single-particle image processing. ATP hydrolysis does not change the conformation of the cis ring, but its effects are transmitted through an inter-ring contact and cause domain rotations in the mobile trans ring. These rigid-body movements in the trans ring lead to disruption of its intra-ring contacts, expansion of the entire ring and opening of both the nucleotide pocket and the substrate-binding domains, admitting ATP and new substrate protein.
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==About this Structure==
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Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes.,Ranson NA, Clare DK, Farr GW, Houldershaw D, Horwich AL, Saibil HR Nat Struct Mol Biol. 2006 Feb;13(2):147-52. Epub 2006 Jan 22. PMID:16429154<ref>PMID:16429154</ref>
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2C7C is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C7C OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes., Ranson NA, Clare DK, Farr GW, Houldershaw D, Horwich AL, Saibil HR, Nat Struct Mol Biol. 2006 Feb;13(2):147-52. Epub 2006 Jan 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16429154 16429154]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 2c7c" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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[[Category: Clare, D.K.]]
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[[Category: Farr, G.W.]]
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[[Category: Horwich, A.L.]]
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[[Category: Houldershaw, D.]]
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[[Category: Ranson, N.A.]]
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[[Category: Saibil, H.R.]]
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[[Category: atomic structure fitting]]
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[[Category: atp-binding]]
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[[Category: cell cycle]]
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[[Category: cell division]]
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[[Category: chaperone]]
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[[Category: chaperonin]]
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[[Category: nucleotide-binding]]
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[[Category: phosphorylation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:01:50 2007''
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==See Also==
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Clare DK]]
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[[Category: Farr GW]]
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[[Category: Horwich AL]]
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[[Category: Houldershaw D]]
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[[Category: Ranson NA]]
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[[Category: Saibil HR]]

Current revision

FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)

2c7c, resolution 7.70Å

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