8AFQ
Tube assembly of Atg18-PR72AA
Summary for 8AFQ
| Entry DOI | 10.2210/pdb8afq/pdb |
| EMDB information | 15408 |
| Descriptor | Autophagy-related protein 18 (1 entity in total) |
| Functional Keywords | autophagy, membrane remodeling, pip binding, pi3p, pi(3, 5)p2, lipid binding protein, membrane protein |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 4 |
| Total formula weight | 220183.11 |
| Authors | Mann, D.,Fromm, S.,Martinez-Sanchez, A.,Gopaldass, N.,Mayer, A.,Sachse, C. (deposition date: 2022-07-18, release date: 2023-11-01, Last modification date: 2024-05-15) |
| Primary citation | Mann, D.,Fromm, S.A.,Martinez-Sanchez, A.,Gopaldass, N.,Choy, R.,Mayer, A.,Sachse, C. Atg18 oligomer organization in assembled tubes and on lipid membrane scaffolds. Nat Commun, 14:8086-8086, 2023 Cited by PubMed Abstract: Autophagy-related protein 18 (Atg18) participates in the elongation of early autophagosomal structures in concert with Atg2 and Atg9 complexes. How Atg18 contributes to the structural coordination of Atg2 and Atg9 at the isolation membrane remains to be understood. Here, we determined the cryo-EM structures of Atg18 organized in helical tubes, Atg18 oligomers in solution as well as on lipid membrane scaffolds. The helical assembly is composed of Atg18 tetramers forming a lozenge cylindrical lattice with remarkable structural similarity to the COPII outer coat. When reconstituted with lipid membranes, using subtomogram averaging we determined tilted Atg18 dimer structures bridging two juxtaposed lipid membranes spaced apart by 80 Å. Moreover, lipid reconstitution experiments further delineate the contributions of Atg18's FRRG motif and the amphipathic helical extension in membrane interaction. The observed structural plasticity of Atg18's oligomeric organization and membrane binding properties provide a molecular framework for the positioning of downstream components of the autophagy machinery. PubMed: 38057304DOI: 10.1038/s41467-023-43460-3 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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