|Title||Structure of the Cdc48 segregase in the act of unfolding an authentic substrate.|
|Journal, issue, pages||Science, Year 2019|
|Publish date||Jun 27, 2019|
|Authors||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 /|
|PubMed 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 ...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 links||PubMed:31249134 / Publisher's page|
|Keywords||MOTOR PROTEIN / Cdc48 / AAA+ ATPase / substrate translocation|
|Methods||EM (single particle)|
|Resolution||3.7 - 4.5 A|
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