22MM22MM の概要
| エントリーDOI | 10.2210/pdb22mm/pdb |
| EMDBエントリー | 68472 |
| 関連するBIRD辞書のPRD_ID | PRD_000907 |
| 分子名称 | 26S proteasome non-ATPase regulatory subunit 1, 26S proteasome complex subunit SEM1, 26S proteasome regulatory subunit 7, ... (38 entities in total) |
| 機能のキーワード | 26s proteasome, midnolin, hydrolase |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| タンパク質・核酸の鎖数 | 46 |
| 化学式量合計 | 1676134.75 |
| 構造登録者 | |
| 主引用文献 | Zhu, C.,Qin, L.,Dai, Z.,Zuo, P.,Yang, A.,Zhong, L.,Lin, Z.,Liang, L. Structural dynamics of the midnolin-proteasome during ubiquitin-independent substrate turnover. Nat Commun, 17:-, 2026 Cited by PubMed Abstract: The 26S proteasome typically degrades proteins marked by ubiquitin chains. However, a distinct, ubiquitin-independent degradation pathway for nuclear proteins exists, mediated by the adaptor protein midnolin, yet its molecular mechanism remains poorly understood. Here, we present nine cryo-electron microscopy structures of the human 26S proteasome in complex with midnolin, which collectively delineate a near-complete catalytic cycle. Our structures reveal that midnolin binds to the proteasome via the RPN1 subunit by its C-terminal helix. Unexpectedly, its ubiquitin-like domain interacts with the RPN11 deubiquitinase in a non-catalytic role. This interaction positions the adjacent Catch domain, which is responsible for substrate binding, directly above the proteasomal entrance, potentially facilitating substrate entry into the proteasome. Furthermore, we observe four consecutive spiral staircase conformations of the AAA+ ATPase hexamer during substrate translocation. These findings provide insights into the mechanisms underlying ubiquitin-independent nuclear protein degradation and may help develop strategies for targeting nuclear proteins via direct proteasomal degradation. PubMed: 41896529DOI: 10.1038/s41467-026-71002-0 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.42 Å) |
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