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- W2954501369 abstract "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." @default.
- W2954501369 created "2019-07-12" @default.
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- W2954501369 date "2019-08-02" @default.
- W2954501369 modified "2023-09-30" @default.
- W2954501369 title "Structure of the Cdc48 segregase in the act of unfolding an authentic substrate" @default.
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- W2954501369 doi "https://doi.org/10.1126/science.aax0486" @default.
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- W2954501369 hasPublicationYear "2019" @default.
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