5ZQ2
SidE apo form
5ZQ2 の概要
| エントリーDOI | 10.2210/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 | |
| 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: 29731171DOI: 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) |
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