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    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. Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.


    Ian Cooney, Han Han, Michael G Stewart, Richard H Carson, Daniel T Hansen, Janet H Iwasa, John C Price, Christopher P Hill, Peter S Shen. Structure of the Cdc48 segregase in the act of unfolding an authentic substrate. Science (New York, N.Y.). 2019 Aug 02;365(6452):502-505

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    PMID: 31249134

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