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TitleStructure of the Cdc48 segregase in the act of unfolding an authentic substrate.
Journal, issue, pagesScience, Vol. 365, Issue 6452, Page 502-505, Year 2019
Publish dateAug 2, 2019
AuthorsIan Cooney / Han Han / Michael G Stewart / Richard H Carson / Daniel T Hansen / Janet H Iwasa / John C Price / Christopher P Hill / Peter S Shen /
PubMed AbstractThe cellular machine Cdc48 functions in multiple biological pathways by segregating its protein substrates from a variety of stable environments such as organelles or multi-subunit complexes. Despite ...The cellular machine Cdc48 functions in multiple biological pathways by segregating its protein substrates from a variety of stable environments such as organelles or multi-subunit complexes. Despite extensive studies, the mechanism of Cdc48 has remained obscure, and its reported structures are inconsistent with models of substrate translocation proposed for other AAA+ ATPases (adenosine triphosphatases). Here, we report a 3.7-angstrom-resolution structure of Cdc48 in complex with an adaptor protein and a native substrate. Cdc48 engages substrate by adopting a helical configuration of substrate-binding residues that extends through the central pore of both of the ATPase rings. These findings indicate a unified hand-over-hand mechanism of protein translocation by Cdc48 and other AAA+ ATPases.
External linksScience / PubMed:31249134 / PubMed Central
MethodsEM (single particle)
Resolution3.7 - 4.5 Å
Structure data

20124

6omb

EMDB-20124: Cdc48 Hexamer
PDB-6omb: Cdc48 Hexamer (Subunits A to E) with substrate bound to the central pore
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-20136:
Cdc48 Hexamer (Focused Classification for Subunit F, state1)
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-20137:
Cdc48 Hexamer (Focused Classification for Subunit F, state2)
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-20138:
Cdc48 Symmetric Hexamer
Method: EM (single particle) / Resolution: 4.5 Å

20149

6opc

EMDB-20149, PDB-6opc:
Cdc48 Hexamer in a complex with substrate and Shp1(Ubx Domain)
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

ChemComp-MG:
Unknown entry

Source
  • saccharomyces cerevisiae s288c (yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsMOTOR PROTEIN / Cdc48 / AAA+ ATPase / substrate translocation

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