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1qvr

From Proteopedia

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[[Image:1qvr.gif|left|200px]]
 
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{{Structure
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==Crystal Structure Analysis of ClpB==
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|PDB= 1qvr |SIZE=350|CAPTION= <scene name='initialview01'>1qvr</scene>, resolution 3.00&Aring;
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<StructureSection load='1qvr' size='340' side='right'caption='[[1qvr]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene> and <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'>ANP</scene>
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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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|ACTIVITY=
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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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|GENE= CLPB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])
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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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}}
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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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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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==Overview==
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*[[3D structures of ClpB|3D structures of ClpB]]
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Molecular chaperones assist protein folding by facilitating their "forward" folding and preventing aggregation. However, once aggregates have formed, these chaperones cannot facilitate protein disaggregation. Bacterial ClpB and its eukaryotic homolog Hsp104 are essential proteins of the heat-shock response, which have the remarkable capacity to rescue stress-damaged proteins from an aggregated state. We have determined the structure of Thermus thermophilus ClpB (TClpB) using a combination of X-ray crystallography and cryo-electron microscopy (cryo-EM). Our single-particle reconstruction shows that TClpB forms a two-tiered hexameric ring. The ClpB/Hsp104-linker consists of an 85 A long and mobile coiled coil that is located on the outside of the hexamer. Our mutagenesis and biochemical data show that both the relative position and motion of this coiled coil are critical for chaperone function. Taken together, we propose a mechanism by which an ATP-driven conformational change is coupled to a large coiled-coil motion, which is indispensable for protein disaggregation.
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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1QVR is a [[Single protein]] structure of 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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</StructureSection>
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[[Category: Large Structures]]
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==Reference==
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The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state., Lee S, Sowa ME, Watanabe YH, Sigler PB, Chiu W, Yoshida M, Tsai FT, Cell. 2003 Oct 17;115(2):229-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14567920 14567920]
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[[Category: Single protein]]
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[[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: ANP]]
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[[Category: PT]]
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[[Category: aaa atpase]]
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[[Category: coiled coil]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:43:20 2008''
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Current revision

Crystal Structure Analysis of ClpB

PDB ID 1qvr

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