1pcq

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[[Image:1pcq.gif|left|200px]]
 
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==Crystal structure of groEL-groES==
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The line below this paragraph, containing "STRUCTURE_1pcq", creates the "Structure Box" on the page.
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<StructureSection load='1pcq' size='340' side='right'caption='[[1pcq]], [[Resolution|resolution]] 2.81&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'>[[1pcq]] 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=1PCQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PCQ 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]] 2.808&#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=AF3:ALUMINUM+FLUORIDE'>AF3</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_1pcq| PDB=1pcq | 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=1pcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pcq OCA], [https://pdbe.org/1pcq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pcq RCSB], [https://www.ebi.ac.uk/pdbsum/1pcq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pcq 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/pc/1pcq_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=1pcq ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of groEL-groES'''
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==See Also==
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*[[Chaperonin|Chaperonin]]
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*[[Chaperonin 3D structures|Chaperonin 3D structures]]
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==Overview==
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__TOC__
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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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</StructureSection>
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==About this Structure==
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1PCQ 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=1PCQ 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: Chaperone]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:56:43 2008''
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Current revision

Crystal structure of groEL-groES

PDB ID 1pcq

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