1gr5

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[[Image:1gr5.gif|left|200px]]
 
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==Solution Structure of apo GroEL by Cryo-Electron microscopy==
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The line below this paragraph, containing "STRUCTURE_1gr5", creates the "Structure Box" on the page.
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<SX load='1gr5' size='340' side='right' viewer='molstar' caption='[[1gr5]], [[Resolution|resolution]] 7.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1gr5]] is a 14 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=1GR5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GR5 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 7.9&#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=1gr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gr5 OCA], [https://pdbe.org/1gr5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gr5 RCSB], [https://www.ebi.ac.uk/pdbsum/1gr5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gr5 ProSAT]</span></td></tr>
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{{STRUCTURE_1gr5| PDB=1gr5 | SCENE= }}
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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/gr/1gr5_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=1gr5 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 chaperonin GroEL drives its protein-folding cycle by cooperatively binding ATP to one of its two rings, priming that ring to become folding-active upon GroES binding, while simultaneously discharging the previous folding chamber from the opposite ring. The GroEL-ATP structure, determined by cryo-EM and atomic structure fitting, shows that the intermediate domains rotate downward, switching their intersubunit salt bridge contacts from substrate binding to ATP binding domains. These observations, together with the effects of ATP binding to a GroEL-GroES-ADP complex, suggest structural models for the ATP-induced reduction in affinity for polypeptide and for cooperativity. The model for cooperativity, based on switching of intersubunit salt bridge interactions around the GroEL ring, may provide general insight into cooperativity in other ring complexes and molecular machines.
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'''SOLUTION STRUCTURE OF APO GROEL BY CRYO-ELECTRON MICROSCOPY'''
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ATP-bound states of GroEL captured by cryo-electron microscopy.,Ranson NA, Farr GW, Roseman AM, Gowen B, Fenton WA, Horwich AL, Saibil HR Cell. 2001 Dec 28;107(7):869-79. PMID:11779463<ref>PMID:11779463</ref>
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==Overview==
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The chaperonin GroEL drives its protein-folding cycle by cooperatively binding ATP to one of its two rings, priming that ring to become folding-active upon GroES binding, while simultaneously discharging the previous folding chamber from the opposite ring. The GroEL-ATP structure, determined by cryo-EM and atomic structure fitting, shows that the intermediate domains rotate downward, switching their intersubunit salt bridge contacts from substrate binding to ATP binding domains. These observations, together with the effects of ATP binding to a GroEL-GroES-ADP complex, suggest structural models for the ATP-induced reduction in affinity for polypeptide and for cooperativity. The model for cooperativity, based on switching of intersubunit salt bridge interactions around the GroEL ring, may provide general insight into cooperativity in other ring complexes and molecular machines.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1GR5 is a [[Single protein]] structure of sequence 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=1GR5 OCA].
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</div>
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<div class="pdbe-citations 1gr5" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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ATP-bound states of GroEL captured by cryo-electron microscopy., Ranson NA, Farr GW, Roseman AM, Gowen B, Fenton WA, Horwich AL, Saibil HR, Cell. 2001 Dec 28;107(7):869-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11779463 11779463]
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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>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Farr, G W.]]
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[[Category: Farr GW]]
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[[Category: Fenton, W A.]]
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[[Category: Fenton WA]]
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[[Category: Gowen, B.]]
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[[Category: Gowen B]]
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[[Category: Horwich, A L.]]
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[[Category: Horwich AL]]
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[[Category: Ranson, N A.]]
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[[Category: Ranson NA]]
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[[Category: Roseman, A M.]]
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[[Category: Roseman AM]]
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[[Category: Saibil, H R.]]
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[[Category: Saibil HR]]
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[[Category: Chaperonin]]
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[[Category: Hsp60 class]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:55:03 2008''
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Current revision

Solution Structure of apo GroEL by Cryo-Electron microscopy

1gr5, resolution 7.90Å

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