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DOI | 10.2210/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: 31249135DOI: 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) |
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