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==Negative-stain electron microscopy of E. coli ClpB of Y503D hyperactive mutant (BAP form bound to ClpP)==
==Negative-stain electron microscopy of E. coli ClpB of Y503D hyperactive mutant (BAP form bound to ClpP)==
<StructureSection load='4d2x' size='340' side='right' caption='[[4d2x]], [[Resolution|resolution]] 20.00&Aring;' scene=''>
<SX load='4d2x' size='340' side='right' viewer='molstar' caption='[[4d2x]], [[Resolution|resolution]] 20.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4d2x]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D2X FirstGlance]. <br>
<table><tr><td colspan='2'>[[4d2x]] is a 6 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=4D2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D2X FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 20&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d2q|4d2q]], [[4d2u|4d2u]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d2x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d2x RCSB], [http://www.ebi.ac.uk/pdbsum/4d2x PDBsum]</span></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=4d2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d2x OCA], [https://pdbe.org/4d2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d2x RCSB], [https://www.ebi.ac.uk/pdbsum/4d2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d2x ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CLPB_ECOLI CLPB_ECOLI]] 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:10982797</ref> <ref>PMID:12624113</ref> <ref>PMID:14640692</ref>
[https://www.uniprot.org/uniprot/CLPB_ECOLI CLPB_ECOLI] 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:10982797</ref> <ref>PMID:12624113</ref> <ref>PMID:14640692</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4d2x" style="background-color:#fffaf0;"></div>
==See Also==
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
*[[3D structures of ClpB|3D structures of ClpB]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</SX>
[[Category: Bukau, B]]
[[Category: Escherichia coli]]
[[Category: Carroni, M]]
[[Category: Large Structures]]
[[Category: Clare, D K]]
[[Category: Bukau B]]
[[Category: Kopp, J]]
[[Category: Carroni M]]
[[Category: Kummer, E]]
[[Category: Clare DK]]
[[Category: Mogk, A]]
[[Category: Kopp J]]
[[Category: Oguchi, Y]]
[[Category: Kummer E]]
[[Category: Saibil, H R]]
[[Category: Mogk A]]
[[Category: Sinning, I]]
[[Category: Oguchi Y]]
[[Category: Wendler, P]]
[[Category: Saibil HR]]
[[Category: Bap]]
[[Category: Sinning I]]
[[Category: Chaperone]]
[[Category: Wendler P]]
[[Category: Clpb]]
[[Category: Coiled- coil domain]]
[[Category: Disaggregase]]
[[Category: Y503d hyperactive mutant]]
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