1qvr: Difference between revisions

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[[Image:1qvr.png|left|200px]]


{{STRUCTURE_1qvr| PDB=1qvr | SCENE= }}
==Crystal Structure Analysis of ClpB==
<StructureSection load='1qvr' size='340' side='right'caption='[[1qvr]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qv/1qvr_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>


===Crystal Structure Analysis of ClpB===
==See Also==
 
*[[Chaperone protein ClpB|Chaperone protein ClpB]]
{{ABSTRACT_PUBMED_14567920}}
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
*[[3D structures of ClpB|3D structures of ClpB]]
==About this Structure==
== References ==
[[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].
<references/>
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:014567920</ref><ref group="xtra">PMID:017009862</ref><references group="xtra"/>
[[Category: Large Structures]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Chiu, W.]]
[[Category: Chiu W]]
[[Category: Lee, S.]]
[[Category: Lee S]]
[[Category: Sigler, P B.]]
[[Category: Sigler PB]]
[[Category: Sowa, M E.]]
[[Category: Sowa ME]]
[[Category: Tsai, F T.F.]]
[[Category: Tsai FTF]]
[[Category: Watanabe, Y.]]
[[Category: Watanabe Y]]
[[Category: Yoshida, M.]]
[[Category: Yoshida M]]
[[Category: Aaa atpase]]
[[Category: Chaperone]]