1pf9

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[[Image:1pf9.gif|left|200px]]
 
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==GroEL-GroES-ADP==
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The line below this paragraph, containing "STRUCTURE_1pf9", creates the "Structure Box" on the page.
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<StructureSection load='1pf9' size='340' side='right'caption='[[1pf9]], [[Resolution|resolution]] 2.99&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'>[[1pf9]] 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=1PF9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PF9 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">X-ray diffraction, [[Resolution|Resolution]] 2.993&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_1pf9| PDB=1pf9 | SCENE= }}
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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=1pf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pf9 OCA], [https://pdbe.org/1pf9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pf9 RCSB], [https://www.ebi.ac.uk/pdbsum/1pf9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pf9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CH10_ECOLI CH10_ECOLI] Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.[HAMAP-Rule:MF_00580]
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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/pf/1pf9_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=1pf9 ConSurf].
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<div style="clear:both"></div>
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'''GroEL-GroES-ADP'''
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==See Also==
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*[[Chaperonin 3D structures|Chaperonin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Productive cis folding by the chaperonin GroEL is triggered by the binding of ATP but not ADP, along with cochaperonin GroES, to the same ring as non-native polypeptide, ejecting polypeptide into an encapsulated hydrophilic chamber. We examined the specific contribution of the gamma-phosphate of ATP to this activation process using complexes of ADP and aluminium or beryllium fluoride. These ATP analogues supported productive cis folding of the substrate protein, rhodanese, even when added to already-formed, folding-inactive cis ADP ternary complexes, essentially introducing the gamma-phosphate of ATP in an independent step. Aluminium fluoride was observed to stabilize the association of GroES with GroEL, with a substantial release of free energy (-46 kcal/mol). To understand the basis of such activation and stabilization, a crystal structure of GroEL-GroES-ADP.AlF3 was determined at 2.8 A. A trigonal AlF3 metal complex was observed in the gamma-phosphate position of the nucleotide pocket of the cis ring. Surprisingly, when this structure was compared with that of the previously determined GroEL-GroES-ADP complex, no other differences were observed. We discuss the likely basis of the ability of gamma-phosphate binding to convert preformed GroEL-GroES-ADP-polypeptide complexes into the folding-active state.
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==About this Structure==
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1PF9 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=1PF9 OCA].
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==Reference==
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Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics., Chaudhry C, Farr GW, Todd MJ, Rye HS, Brunger AT, Adams PD, Horwich AL, Sigler PB, EMBO J. 2003 Oct 1;22(19):4877-87. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14517228 14517228]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Adams, P D.]]
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[[Category: Adams PD]]
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[[Category: Brunger, A T.]]
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[[Category: Brunger AT]]
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[[Category: Chaudhry, C.]]
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[[Category: Chaudhry C]]
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[[Category: Farr, G W.]]
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[[Category: Farr GW]]
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[[Category: Horwich, A L.]]
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[[Category: Horwich AL]]
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[[Category: Rye, H S.]]
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[[Category: Rye HS]]
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[[Category: Sigler, P B.]]
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[[Category: Sigler PB]]
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[[Category: Todd, M J.]]
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[[Category: Todd MJ]]
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[[Category: Chaperonin]]
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[[Category: Co-chaperonin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:00:56 2008''
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Current revision

GroEL-GroES-ADP

PDB ID 1pf9

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