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6oax

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==Structure of the hyperactive ClpB mutant K476C, bound to casein, pre-state==
==Structure of the hyperactive ClpB mutant K476C, bound to casein, pre-state==
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<StructureSection load='6oax' size='340' side='right'caption='[[6oax]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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<SX load='6oax' size='340' side='right' viewer='molstar' caption='[[6oax]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6oax]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OAX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OAX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6oax]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OAX FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6oay|6oay]], [[6og1|6og1]], [[6og2|6og2]], [[6og3|6og3]]</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=6oax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oax OCA], [https://pdbe.org/6oax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oax RCSB], [https://www.ebi.ac.uk/pdbsum/6oax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oax ProSAT]</span></td></tr>
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<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=6oax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oax OCA], [http://pdbe.org/6oax PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oax RCSB], [http://www.ebi.ac.uk/pdbsum/6oax PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oax ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[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>
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Bacterial ClpB and yeast Hsp104 are homologous Hsp100 protein disaggregases that serve critical functions in proteostasis by solubilizing protein aggregates. Two AAA+ nucleotide binding domains (NBDs) power polypeptide translocation through a central channel comprised of a hexameric spiral of protomers that contact substrate via conserved pore-loop interactions. Here we report cryo-EM structures of a hyperactive ClpB variant bound to the model substrate, casein in the presence of slowly hydrolysable ATPgammaS, which reveal the translocation mechanism. Distinct substrate-gripping interactions are identified for NBD1 and NBD2 pore loops. A trimer of N-terminal domains define a channel entrance that binds the polypeptide substrate adjacent to the topmost NBD1 contact. NBD conformations at the seam interface reveal how ATP hydrolysis-driven substrate disengagement and re-binding are precisely tuned to drive a directional, stepwise translocation cycle.
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Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase.,Rizo AN, Lin J, Gates SN, Tse E, Bart SM, Castellano LM, DiMaio F, Shorter J, Southworth DR Nat Commun. 2019 Jun 3;10(1):2393. doi: 10.1038/s41467-019-10150-y. PMID:31160557<ref>PMID:31160557</ref>
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==See Also==
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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*[[3D structures of ClpB|3D structures of ClpB]]
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</div>
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<div class="pdbe-citations 6oax" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bart, S M]]
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[[Category: Bart SM]]
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[[Category: Castellano, L M]]
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[[Category: Castellano LM]]
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[[Category: Dimaio, F]]
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[[Category: Dimaio F]]
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[[Category: Gates, S N]]
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[[Category: Gates SN]]
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[[Category: Lin, J B]]
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[[Category: Lin J-B]]
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[[Category: Rizo, A R]]
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[[Category: Rizo AR]]
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[[Category: Shorter, J]]
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[[Category: Shorter J]]
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[[Category: Southworth, D R]]
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[[Category: Southworth DR]]
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[[Category: Tse, E]]
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[[Category: Tse E]]
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[[Category: Aaa+]]
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[[Category: Chaperone]]
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[[Category: Clpb]]
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[[Category: Disaggregase]]
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Current revision

Structure of the hyperactive ClpB mutant K476C, bound to casein, pre-state

6oax, resolution 2.90Å

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