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5ZQ2

SidE apo form

5ZQ2 の概要
エントリーDOI10.2210/pdb5zq2/pdb
分子名称SidE (2 entities in total)
機能のキーワードubiquitination, cell invasion
由来する生物種Legionella pneumophila
タンパク質・核酸の鎖数2
化学式量合計192032.25
構造登録者
Wang, Y.,Gao, A.,Gao, P. (登録日: 2018-04-17, 公開日: 2018-05-23, 最終更新日: 2023-11-29)
主引用文献Wang, Y.,Shi, M.,Feng, H.,Zhu, Y.,Liu, S.,Gao, A.,Gao, P.
Structural Insights into Non-canonical Ubiquitination Catalyzed by SidE.
Cell, 173:1231-1243.e16, 2018
Cited by
PubMed Abstract: Ubiquitination constitutes one of the most important signaling mechanisms in eukaryotes. Conventional ubiquitination is catalyzed by the universally conserved E1-E2-E3 three-enzyme cascade in an ATP-dependent manner. The newly identified SidE family effectors of the pathogen Legionella pneumophila ubiquitinate several human proteins by a different mechanism without engaging any of the conventional ubiquitination machinery. We now report the crystal structures of SidE alone and in complex with ubiquitin, NAD, and ADP-ribose, thereby capturing different conformations of SidE before and after ubiquitin and ligand binding. The structures of ubiquitin bound to both mART and PDE domains reveal several unique features of the two reaction steps catalyzed by SidE. Further, the structural and biochemical results demonstrate that SidE family members do not recognize specific structural folds of the substrate proteins. Our studies provide both structural explanations for the functional observations and new insights into the molecular mechanisms of this non-canonical ubiquitination machinery.
PubMed: 29731171
DOI: 10.1016/j.cell.2018.04.023
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.704 Å)
構造検証レポート
Validation report summary of 5zq2
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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