5JHC

Crystal structure of the self-assembled propeptides from Ape1

Summary for 5JHC

• Entry DOI: 10.2210/pdb5jhc/pdb
• Related: 5JGF 5JH9
• Descriptor: Vacuolar aminopeptidase 1 (1 entity in total)
• Functional Keywords: trimeric coiled-coil, hydrolase
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Total number of polymer chains: 39
• Total formula weight: 111554.31

Authors

Yamasaki, A.,Noda, N.N. (deposition date: 2016-04-20, release date: 2016-06-29, Last modification date: 2024-03-20)

Primary citation

Yamasaki, A.,Watanabe, Y.,Adachi, W.,Suzuki, K.,Matoba, K.,Kirisako, H.,Kumeta, H.,Nakatogawa, H.,Ohsumi, Y.,Inagaki, F.,Noda, N.N.
Structural Basis for Receptor-Mediated Selective Autophagy of Aminopeptidase I Aggregates
Cell Rep, 16:19-27, 2016

PubMed Abstract: 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.

PubMed: 27320913
DOI: 10.1016/j.celrep.2016.05.066

Experimental method

X-RAY DIFFRACTION (3.4 Å)