3VX8

Crystal structure of Arabidopsis thaliana Atg7NTD-Atg3 complex

3VX8 の概要

• エントリーDOI: 10.2210/pdb3vx8/pdb
• 関連するPDBエントリー: 3VX6 3VX7
• 分子名称: Ubiquitin-like modifier-activating enzyme atg7, Autophagy-related protein 3 (3 entities in total)
• 機能のキーワード: e1-e2 complex, ligase
• 由来する生物種: Arabidopsis thaliana (mouse-ear cress); 詳細
• 細胞内の位置: Cytoplasm (Probable): Q0WWQ1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 138046.51

構造登録者

Matoba, K.,Fujioka, Y.,Noda, N.N. (登録日: 2012-09-11, 公開日: 2012-11-14, 最終更新日: 2023-10-18)

主引用文献

Yamaguchi, M.,Matoba, K.,Sawada, R.,Fujioka, Y.,Nakatogawa, H.,Yamamoto, H.,Kobashigawa, Y.,Hoshida, H.,Akada, R.,Ohsumi, Y.,Noda, N.N.,Inagaki, F.
Noncanonical recognition and UBL loading of distinct E2s by autophagy-essential Atg7.
Nat.Struct.Mol.Biol., 19:1250-1256, 2012

PubMed Abstract: Autophagy requires ubiquitin-like Atg8 and Atg12 conjugation systems, where Atg7 has a critical role as the sole E1 enzyme. Although Atg7 recognizes two distinct E2s, Atg3 and Atg10, it is not understood how Atg7 correctly loads these E2s with their cognate ubiquitin-like proteins, Atg8 and Atg12. Here, we report the crystal structures of the N-terminal domain of Atg7 bound to Atg10 or Atg3 of thermotolerant yeast and plant homologs. The observed Atg7-Atg10 and Atg7-Atg3 interactions, which resemble each other but are quite distinct from the canonical E1-E2 interaction, makes Atg7 suitable for transferring Atg12 to Atg10 and Atg8 to Atg3 by a trans mechanism. Notably, in vitro experiments showed that Atg7 loads Atg3 and Atg10 with Atg8 and Atg12 in a nonspecific manner, which suggests that cognate conjugate formation in vivo is not an intrinsic quality of Atg7.

PubMed: 23142983
DOI: 10.1038/nsmb.2451

実験手法

X-RAY DIFFRACTION (3.11 Å)