6A9J

Crystal structure of the PE-bound N-terminal domain of Atg2

Summary for 6A9J

• Entry DOI: 10.2210/pdb6a9j/pdb
• Descriptor: Endolysin,Autophagy-related protein 2, 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (2 entities in total)
• Functional Keywords: lipid transport
• Biological source: Enterobacteria phage RB59; More
• Total number of polymer chains: 2
• Total formula weight: 88543.51

Authors

Osawa, T.,Noda, N.N. (deposition date: 2018-07-13, release date: 2019-03-20, Last modification date: 2023-11-22)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.7 Å)