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Structure paper

TitleStructure of the Cdc48 segregase in the act of unfolding an authentic substrate.
Journal, issue, pagesScience, Year 2019
Publish dateJun 27, 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. Here, we report a 3.7 Å 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 linksPubMed:31249134 / Publisher's page
KeywordsMOTOR PROTEIN / Cdc48 / AAA+ ATPase / substrate translocation
MethodsEM (single particle)
Resolution3.7 - 4.5 A
Structure data

EMDB-20124:
Cdc48 Hexamer

EMDB-20136:
Cdc48 Hexamer (Focused Classification for Subunit F, state1)

EMDB-20138:
Cdc48 Symmetric Hexamer

EMDB-20149:
Cdc48 Hexamer in a complex with substrate and Shp1(Ubx Domain)

EMDB-20137:
Cdc48 Hexamer (Focused Classification for Subunit F, state2)

PDB-6opc:
Cdc48 Hexamer in a complex with substrate and Shp1(Ubx Domain)

PDB-6omb:
Cdc48 Hexamer (Subunits A to E) with substrate bound to the central pore

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATEAdenosine diphosphate

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

ChemComp-MG:
MAGNESIUM IONMagnesium

Source
  • saccharomyces cerevisiae s288c (yeast)
  • Baker's yeast (baker's yeast)
  • saccharomyces cerevisiae (baker's yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)

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