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-Structure paper
タイトル | Structure of the Cdc48 segregase in the act of unfolding an authentic substrate. |
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ジャーナル・号・ページ | Science, Vol. 365, Issue 6452, Page 502-505, Year 2019 |
掲載日 | 2019年8月2日 |
著者 | 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 要旨 | 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 (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. |
リンク | Science / PubMed:31249134 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.7 - 4.5 Å |
構造データ | EMDB-20124: Cdc48 Hexamer EMDB-20136: EMDB-20137: EMDB-20138: EMDB-20149, PDB-6opc: |
化合物 | ChemComp-ADP: ChemComp-BEF: ChemComp-MG: |
由来 |
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キーワード | MOTOR PROTEIN (モータータンパク質) / Cdc48 / AAA+ ATPase / substrate translocation |