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6REY

Human 20S-PA200 Proteasome Complex

6REY の概要
エントリーDOI10.2210/pdb6rey/pdb
EMDBエントリー4860
分子名称Proteasome subunit alpha type-6, Proteasome subunit beta type-3, Proteasome subunit beta type-2, ... (17 entities in total)
機能のキーワードproteasome, pa200, activator, hydrolase
由来する生物種Homo sapiens (Human)
詳細
タンパク質・核酸の鎖数30
化学式量合計1143898.08
構造登録者
Toste Rego, A.,da Fonseca, P.C.A. (登録日: 2019-04-12, 公開日: 2019-09-04, 最終更新日: 2024-05-22)
主引用文献Toste Rego, A.,da Fonseca, P.C.A.
Characterization of Fully Recombinant Human 20S and 20S-PA200 Proteasome Complexes.
Mol.Cell, 76:138-147.e5, 2019
Cited by
PubMed Abstract: Proteasomes are essential in all eukaryotic cells. However, their function and regulation remain considerably elusive, particularly those of less abundant variants. We demonstrate the human 20S proteasome recombinant assembly and confirmed the recombinant complex integrity biochemically and with a 2.6 Å resolution cryo-EM map. To assess its competence to form higher-order assemblies, we prepared and analyzed recombinant human 20S-PA200, a poorly characterized nuclear complex. Its 3.0 Å resolution cryo-EM structure reveals the PA200 unique architecture; the details of its intricate interactions with the proteasome, resulting in unparalleled proteasome α ring rearrangements; and the molecular basis for PA200 allosteric modulation of the proteasome active sites. Non-protein cryo-EM densities could be assigned to PA200-bound inositol phosphates, and we speculate regarding their functional role. Here we open extensive opportunities to study the fundamental properties of the diverse and distinct eukaryotic proteasome variants and to improve proteasome targeting under different therapeutic conditions.
PubMed: 31473102
DOI: 10.1016/j.molcel.2019.07.014
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3 Å)
構造検証レポート
Validation report summary of 6rey
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2026-04-22に公開中

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