8FKM
Human Atg3 with deletions of residues 1 to 25 and 90 to 190
8FKM の概要
| エントリーDOI | 10.2210/pdb8fkm/pdb |
| NMR情報 | BMRB: 31065 |
| 分子名称 | Ubiquitin-like-conjugating enzyme ATG3 (1 entity in total) |
| 機能のキーワード | conjugase, atg3, autophagy, ligase |
| 由来する生物種 | Homo sapiens (human) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 22091.42 |
| 構造登録者 | |
| 主引用文献 | Ye, Y.,Tyndall, E.R.,Bui, V.,Bewley, M.C.,Wang, G.,Hong, X.,Shen, Y.,Flanagan, J.M.,Wang, H.G.,Tian, F. Multifaceted membrane interactions of human Atg3 promote LC3-phosphatidylethanolamine conjugation during autophagy. Nat Commun, 14:5503-5503, 2023 Cited by PubMed Abstract: Autophagosome formation, a crucial step in macroautophagy (autophagy), requires the covalent conjugation of LC3 proteins to the amino headgroup of phosphatidylethanolamine (PE) lipids. Atg3, an E2-like enzyme, catalyzes the transfer of LC3 from LC3-Atg3 to PEs in targeted membranes. Here we show that the catalytically important C-terminal regions of human Atg3 (hAtg3) are conformationally dynamic and directly interact with the membrane, in collaboration with its N-terminal membrane curvature-sensitive helix. The functional relevance of these interactions was confirmed by in vitro conjugation and in vivo cellular assays. Therefore, highly curved phagophoric rims not only serve as a geometric cue for hAtg3 recruitment, but also their interaction with hAtg3 promotes LC3-PE conjugation by targeting its catalytic center to the membrane surface and bringing substrates into proximity. Our studies advance the notion that autophagosome biogenesis is directly guided by the spatial interactions of Atg3 with highly curved phagophoric rims. PubMed: 37679347DOI: 10.1038/s41467-023-41243-4 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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