5JH9: Crystal Structure Of Prape1

Selective autophagy mediates the degradation of various cargoes, including protein aggregates and organelles, thereby contributing to cellular homeostasis. Cargo receptors ensure selectivity by tethering specific cargo to lipidated Atg8 at the isolation membrane. However, little is known about the structural requirements underlying receptor-mediated cargo recognition. Here, we report structural, biochemical, and cell biological analysis of the major selective cargo protein in budding yeast, aminopeptidase I (Ape1), and its complex with the receptor Atg19. The Ape1 propeptide has a trimeric coiled-coil structure, which tethers dodecameric Ape1 bodies together to form large aggregates. Atg19 disassembles the propeptide trimer and forms a 2:1 heterotrimer, which not only blankets the Ape1 aggregates but also regulates their size. These receptor activities may promote elongation of the isolation membrane along the aggregate surface, enabling sequestration of the cargo with high specificity.
PDB ID: 5JH9Download
MMDB ID: 140572
PDB Deposition Date: 2016/4/20
Updated in MMDB: 2016/08
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
Similar Structures:
Biological Unit for 5JH9: dodecameric; determined by author and by software (PISA)
Molecular Components in 5JH9
Label Count Molecule
Proteins (12 molecules)
Vacuolar Aminopeptidase 1(Gene symbol: APE1)
Molecule annotation
Chemicals (48 molecules)
* Click molecule labels to explore molecular sequence information.

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