5JGF

Crystal structure of mApe1

5JGF の概要

• エントリーDOI: 10.2210/pdb5jgf/pdb
• 分子名称: Vacuolar aminopeptidase 1, ZINC ION (3 entities in total)
• 機能のキーワード: tetrahedral dodecamer, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 209238.58

構造登録者

Noda, N.N.,Adachi, W.,Inagaki, F. (登録日: 2016-04-20, 公開日: 2016-06-29, 最終更新日: 2023-11-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.83 Å)