2DYT

The crystal structure of Saccharomyces cerevisiae Atg3

2DYT の概要

• エントリーDOI: 10.2210/pdb2dyt/pdb
• 分子名称: Autophagy-related protein 3, SULFATE ION (3 entities in total)
• 機能のキーワード: e2 fold, ligase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm: P40344
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36263.29

構造登録者

Yamada, Y.,Suzuki, N.N.,Inagaki, F. (登録日: 2006-09-17, 公開日: 2007-01-23, 最終更新日: 2024-03-13)

主引用文献

Yamada, Y.,Suzuki, N.N.,Hanada, T.,Ichimura, Y.,Kumeta, H.,Fujioka, Y.,Ohsumi, Y.,Inagaki, F.
The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation
J.Biol.Chem., 282:8036-8043, 2007

PubMed Abstract: Atg3 is an E2-like enzyme that catalyzes the conjugation of Atg8 and phosphatidylethanolamine (PE). The Atg8-PE conjugate is essential for autophagy, which is the bulk degradation process of cytoplasmic components by the vacuolar/lysosomal system. We report here the crystal structure of Saccharomyces cerevisiae Atg3 at 2.5-A resolution. Atg3 has an alpha/beta-fold, and its core region is topologically similar to canonical E2 enzymes. Atg3 has two regions inserted in the core region, one of which consists of approximately 80 residues and has a random coil structure in solution and another with a long alpha-helical structure that protrudes from the core region as far as 30 A. In vivo and in vitro analyses suggested that the former region is responsible for binding Atg7, an E1-like enzyme, and that the latter is responsible for binding Atg8. A sulfate ion was bound near the catalytic cysteine of Atg3, suggesting a possible binding site for the phosphate moiety of PE. The structure of Atg3 provides a molecular basis for understanding the unique lipidation reaction that Atg3 carries out.

PubMed: 17227760
DOI: 10.1074/jbc.M611473200

実験手法

X-RAY DIFFRACTION (2.5 Å)