1qvr

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[[Image:1qvr.png|left|200px]]
 
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{{STRUCTURE_1qvr| PDB=1qvr | SCENE= }}
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==Crystal Structure Analysis of ClpB==
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<StructureSection load='1qvr' size='340' side='right'caption='[[1qvr]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qvr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QVR 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=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</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=1qvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qvr OCA], [https://pdbe.org/1qvr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qvr RCSB], [https://www.ebi.ac.uk/pdbsum/1qvr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qvr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CLPB_THET8 CLPB_THET8] Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK.<ref>PMID:10377389</ref>
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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/qv/1qvr_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=1qvr ConSurf].
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<div style="clear:both"></div>
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===Crystal Structure Analysis of ClpB===
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==See Also==
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*[[Chaperone protein ClpB|Chaperone protein ClpB]]
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{{ABSTRACT_PUBMED_14567920}}
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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*[[3D structures of ClpB|3D structures of ClpB]]
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==About this Structure==
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== References ==
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[[1qvr]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QVR OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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<ref group="xtra">PMID:014567920</ref><ref group="xtra">PMID:017009862</ref><references group="xtra"/>
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[[Category: Large Structures]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: Chiu, W.]]
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[[Category: Chiu W]]
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[[Category: Lee, S.]]
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[[Category: Lee S]]
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[[Category: Sigler, P B.]]
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[[Category: Sigler PB]]
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[[Category: Sowa, M E.]]
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[[Category: Sowa ME]]
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[[Category: Tsai, F T.F.]]
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[[Category: Tsai FTF]]
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[[Category: Watanabe, Y.]]
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[[Category: Watanabe Y]]
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[[Category: Yoshida, M.]]
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[[Category: Yoshida M]]
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[[Category: Aaa atpase]]
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[[Category: Chaperone]]
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Current revision

Crystal Structure Analysis of ClpB

PDB ID 1qvr

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