2c7c: Difference between revisions

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[[Image:2c7c.gif|left|200px]]
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{{STRUCTURE_2c7c|  PDB=2c7c  |  SCENE=  }}
'''FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)'''


==FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)==
<SX load='2c7c' size='340' side='right' viewer='molstar' caption='[[2c7c]], [[Resolution|resolution]] 7.70&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</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/c7/2c7c_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=2c7c ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2C7C is a [[Protein complex]] structure of sequences from [http://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].
</div>
<div class="pdbe-citations 2c7c" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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://www.ncbi.nlm.nih.gov/pubmed/16429154 16429154]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
</SX>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Clare, D K.]]
[[Category: Clare DK]]
[[Category: Farr, G W.]]
[[Category: Farr GW]]
[[Category: Horwich, A L.]]
[[Category: Horwich AL]]
[[Category: Houldershaw, D.]]
[[Category: Houldershaw D]]
[[Category: Ranson, N A.]]
[[Category: Ranson NA]]
[[Category: Saibil, H R.]]
[[Category: Saibil HR]]
[[Category: Atomic structure fitting]]
[[Category: Atp-binding]]
[[Category: Cell cycle]]
[[Category: Cell division]]
[[Category: Chaperone]]
[[Category: Chaperonin]]
[[Category: Nucleotide-binding]]
[[Category: Phosphorylation]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 21:22:32 2008''

Latest revision as of 12:22, 9 May 2024

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

2c7c, resolution 7.70Å

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