6oay
From Proteopedia
(Difference between revisions)
Line 9: | Line 9: | ||
<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=6oay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oay OCA], [http://pdbe.org/6oay PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oay RCSB], [http://www.ebi.ac.uk/pdbsum/6oay PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oay ProSAT]</span></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=6oay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oay OCA], [http://pdbe.org/6oay PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oay RCSB], [http://www.ebi.ac.uk/pdbsum/6oay PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oay ProSAT]</span></td></tr> | ||
</table> | </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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 6oay" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 06:36, 19 June 2019
Structure of the hyperactive ClpB mutant K476C, bound to casein, post-state
|
Categories: Bos taurus | Large Structures | Bart, S M | Castellano, L M | Dimaio, F | Gates, S N | Lin, J B | Rizo, A R | Shorter, J | Southworth, D R | Tse, E | Aaa+ | Chaperone | Clpb | Disaggregase