6og2: Difference between revisions

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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=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>

</table>

== Publication Abstract from PubMed ==

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.

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>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

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@@ Line 8: / Line 8: @@
 <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=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>
 </table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6og2" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>