6A9E

Crystal structure of the N-terminal domain of Atg2

6A9E の概要

• エントリーDOI: 10.2210/pdb6a9e/pdb
• 分子名称: Endolysin,Autophagy-related protein 2 (1 entity in total)
• 機能のキーワード: lipid transport
• 由来する生物種: Enterobacteria phage RB59; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 88180.92

構造登録者

Osawa, T.,Noda, N.N. (登録日: 2018-07-13, 公開日: 2019-03-20, 最終更新日: 2024-10-09)

主引用文献

Osawa, T.,Kotani, T.,Kawaoka, T.,Hirata, E.,Suzuki, K.,Nakatogawa, H.,Ohsumi, Y.,Noda, N.N.
Atg2 mediates direct lipid transfer between membranes for autophagosome formation.
Nat. Struct. Mol. Biol., 26:281-288, 2019

PubMed Abstract: A key event in autophagy is autophagosome formation, whereby the newly synthesized isolation membrane (IM) expands to form a complete autophagosome using endomembrane-derived lipids. Atg2 physically links the edge of the expanding IM with the endoplasmic reticulum (ER), a role that is essential for autophagosome formation. However, the molecular function of Atg2 during ER-IM contact remains unclear, as does the mechanism of lipid delivery to the IM. Here we show that the conserved amino-terminal region of Schizosaccharomyces pombe Atg2 includes a lipid-transfer-protein-like hydrophobic cavity that accommodates phospholipid acyl chains. Atg2 bridges highly curved liposomes, thereby facilitating efficient phospholipid transfer in vitro, a function that is inhibited by mutations that impair autophagosome formation in vivo. These results suggest that Atg2 acts as a lipid-transfer protein that supplies phospholipids for autophagosome formation.

PubMed: 30911189
DOI: 10.1038/s41594-019-0203-4

実験手法

X-RAY DIFFRACTION (3.205 Å)