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6og2

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Current revision (09:24, 20 March 2024) (edit) (undo)
 
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<SX load='6og2' size='340' side='right' viewer='molstar' caption='[[6og2]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
<SX load='6og2' size='340' side='right' viewer='molstar' caption='[[6og2]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6og2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OG2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6OG2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6og2]] is a 2 chain structure with sequence from [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=6OG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OG2 FirstGlance]. <br>
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</td></tr><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></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]] 4.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6og1|6og1]], [[6og3|6og3]], [[6oax|6oax]], [[6oay|6oay]]</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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6og2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6og2 OCA], [http://pdbe.org/6og2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6og2 RCSB], [http://www.ebi.ac.uk/pdbsum/6og2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6og2 ProSAT]</span></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=6og2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6og2 OCA], [https://pdbe.org/6og2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6og2 RCSB], [https://www.ebi.ac.uk/pdbsum/6og2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6og2 ProSAT]</span></td></tr>
</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 6og2" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</SX>
</SX>
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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

Focus classification structure of the hyperactive ClpB mutant K476C, bound to casein, post-state

6og2, resolution 4.10Å

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