1aon

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[[Image:1aon.jpg|left|200px]]<br /><applet load="1aon" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1aon, resolution 3.0&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE ASYMMETRIC CHAPERONIN COMPLEX GROEL/GROES/(ADP)7'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE ASYMMETRIC CHAPERONIN COMPLEX GROEL/GROES/(ADP)7==
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Chaperonins assist protein folding with the consumption of ATP. They exist, as multi-subunit protein assemblies comprising rings of subunits stacked, back to back. In Escherichia coli, asymmetric intermediates of GroEL are, formed with the co-chaperonin GroES and nucleotides bound only to one of, the seven-subunit rings (the cis ring) and not to the opposing ring (the, trans ring). The structure of the GroEL-GroES-(ADP)7 complex reveals how, large en bloc movements of the cis ring's intermediate and apical domains, enable bound GroES to stabilize a folding chamber with ADP confined to the, cis ring. Elevation and twist of the apical domains double the volume of, the central cavity and bury hydrophobic peptide-binding residues in the, interface with GroES, as well as between GroEL subunits, leaving a, hydrophilic cavity lining that is conducive to protein folding. An inward, tilt of the cis equatorial domain causes an outward tilt in the trans ring, that opposes the binding of a second GroES. When combined with new, functional results, this negative allosteric mechanism suggests a model, for an ATP-driven folding cycle that requires a double toroid.
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<StructureSection load='1aon' size='340' side='right'caption='[[1aon]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1aon]] is a 21 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The August 2002 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Chaperones'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2002_8 10.2210/rcsb_pdb/mom_2002_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AON 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">X-ray diffraction, [[Resolution|Resolution]] 3&#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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aon OCA], [https://pdbe.org/1aon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aon RCSB], [https://www.ebi.ac.uk/pdbsum/1aon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aon 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/ao/1aon_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=1aon 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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Chaperonins assist protein folding with the consumption of ATP. They exist as multi-subunit protein assemblies comprising rings of subunits stacked back to back. In Escherichia coli, asymmetric intermediates of GroEL are formed with the co-chaperonin GroES and nucleotides bound only to one of the seven-subunit rings (the cis ring) and not to the opposing ring (the trans ring). The structure of the GroEL-GroES-(ADP)7 complex reveals how large en bloc movements of the cis ring's intermediate and apical domains enable bound GroES to stabilize a folding chamber with ADP confined to the cis ring. Elevation and twist of the apical domains double the volume of the central cavity and bury hydrophobic peptide-binding residues in the interface with GroES, as well as between GroEL subunits, leaving a hydrophilic cavity lining that is conducive to protein folding. An inward tilt of the cis equatorial domain causes an outward tilt in the trans ring that opposes the binding of a second GroES. When combined with new functional results, this negative allosteric mechanism suggests a model for an ATP-driven folding cycle that requires a double toroid.
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==About this Structure==
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The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex.,Xu Z, Horwich AL, Sigler PB Nature. 1997 Aug 21;388(6644):741-50. PMID:9285585<ref>PMID:9285585</ref>
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1AON is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1AON with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb32_1.html Chaperones]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AON 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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The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex., Xu Z, Horwich AL, Sigler PB, Nature. 1997 Aug 21;388(6644):741-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9285585 9285585]
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</div>
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<div class="pdbe-citations 1aon" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Chaperonin 3D structures|Chaperonin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Chaperones]]
[[Category: Chaperones]]
[[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: Horwich, A.L.]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Sigler, P.B.]]
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[[Category: Horwich AL]]
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[[Category: Xu, Z.]]
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[[Category: Sigler PB]]
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[[Category: ADP]]
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[[Category: Xu Z]]
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[[Category: MG]]
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[[Category: chaperonin assisted protein folding]]
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[[Category: complex (groel/groes)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:29:41 2008''
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Current revision

CRYSTAL STRUCTURE OF THE ASYMMETRIC CHAPERONIN COMPLEX GROEL/GROES/(ADP)7

PDB ID 1aon

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