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6OAA

Cdc48-Npl4 complex processing poly-ubiquitinated substrate in the presence of ADP-BeFx, state 1

6OAA の概要
エントリーDOI10.2210/pdb6oaa/pdb
EMDBエントリー0665 0666 20000
分子名称Cell division control protein 48, Nuclear protein localization protein 4, Ubiquitin, ... (5 entities in total)
機能のキーワードatpase, atpase complex, ubiquitin, quality control, motor protein
由来する生物種Saccharomyces cerevisiae S288C (Baker's yeast)
詳細
タンパク質・核酸の鎖数6
化学式量合計446672.14
構造登録者
Twomey, E.C.,Ji, Z.,Wales, T.E.,Bodnar, N.O.,Engen, J.R.,Rapoport, T.A. (登録日: 2019-03-15, 公開日: 2019-07-03, 最終更新日: 2024-03-20)
主引用文献Twomey, E.C.,Ji, Z.,Wales, T.E.,Bodnar, N.O.,Ficarro, S.B.,Marto, J.A.,Engen, J.R.,Rapoport, T.A.
Substrate processing by the Cdc48 ATPase complex is initiated by ubiquitin unfolding.
Science, 365:-, 2019
Cited by
PubMed Abstract: The Cdc48 adenosine triphosphatase (ATPase) (p97 or valosin-containing protein in mammals) and its cofactor Ufd1/Npl4 extract polyubiquitinated proteins from membranes or macromolecular complexes for subsequent degradation by the proteasome. How Cdc48 processes its diverse and often well-folded substrates is unclear. Here, we report cryo-electron microscopy structures of the Cdc48 ATPase in complex with Ufd1/Npl4 and polyubiquitinated substrate. The structures show that the Cdc48 complex initiates substrate processing by unfolding a ubiquitin molecule. The unfolded ubiquitin molecule binds to Npl4 and projects its N-terminal segment through both hexameric ATPase rings. Pore loops of the second ring form a staircase that acts as a conveyer belt to move the polypeptide through the central pore. Inducing the unfolding of ubiquitin allows the Cdc48 ATPase complex to process a broad range of substrates.
PubMed: 31249135
DOI: 10.1126/science.aax1033
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (4.1 Å)
構造検証レポート
Validation report summary of 6oaa
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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