EMD-21874

Single-particle
2.8 Å
EMD-21874 Deposition: 29/04/2020
Map released: 08/07/2020
Last modified: 06/03/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-21874

Structure of human ATG9A, the only transmembrane protein of the core autophagy machinery

EMD-21874

Single-particle
2.8 Å
EMD-21874 Deposition: 29/04/2020
Map released: 08/07/2020
Last modified: 06/03/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Homo sapiens
Sample: Autophagy Related 9A with LMNG
Fitted models: 6wqz (Avg. Q-score: 0.5)

Deposition Authors: Guardia CM , Tan X
Structure of Human ATG9A, the Only Transmembrane Protein of the Core Autophagy Machinery.
PUBMED: 32610138
DOI: doi:10.1016/j.celrep.2020.107837
ISSN: 2211-1247
Abstract:
Autophagy is a catabolic process involving capture of cytoplasmic materials into double-membraned autophagosomes that subsequently fuse with lysosomes for degradation of the materials by lysosomal hydrolases. One of the least understood components of the autophagy machinery is the transmembrane protein ATG9. Here, we report a cryoelectron microscopy structure of the human ATG9A isoform at 2.9-Å resolution. The structure reveals a fold with a homotrimeric domain-swapped architecture, multiple membrane spans, and a network of branched cavities, consistent with ATG9A being a membrane transporter. Mutational analyses support a role for the cavities in the function of ATG9A. In addition, structure-guided molecular simulations predict that ATG9A causes membrane bending, explaining the localization of this protein to small vesicles and highly curved edges of growing autophagosomes.