3VH3

Crystal structure of Atg7CTD-Atg8 complex

3VH3 の概要

• エントリーDOI: 10.2210/pdb3vh3/pdb
• 関連するPDBエントリー: 3VH1 3VH2 3VH4
• 分子名称: Ubiquitin-like modifier-activating enzyme ATG7, Autophagy-related protein 8, ZINC ION, ... (4 entities in total)
• 機能のキーワード: autophagy, e1, zinc binding, metal binding protein-protein transport complex, metal binding protein/protein transport
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• 細胞内の位置: Cytoplasm: P38862; Cytoplasmic vesicle, cvt vesicle membrane; Lipid-anchor: P38182
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51968.13

構造登録者

Noda, N.N.,Satoo, K.,Inagaki, F. (登録日: 2011-08-23, 公開日: 2011-09-21, 最終更新日: 2023-11-08)

主引用文献

Noda, N.N.,Satoo, K.,Fujioka, Y.,Kumeta, H.,Ogura, K.,Nakatogawa, H.,Ohsumi, Y.,Inagaki, F.
Structural basis of Atg8 activation by a homodimeric E1, Atg7.
Mol.Cell, 44:462-475, 2011

PubMed Abstract: E1 enzymes activate ubiquitin-like proteins and transfer them to cognate E2 enzymes. Atg7, a noncanonical E1, activates two ubiquitin-like proteins, Atg8 and Atg12, and plays a crucial role in autophagy. Here, we report crystal structures of full-length Atg7 and its C-terminal domain bound to Atg8 and MgATP, as well as a solution structure of Atg8 bound to the extreme C-terminal domain (ECTD) of Atg7. The unique N-terminal domain (NTD) of Atg7 is responsible for Atg3 (E2) binding, whereas its C-terminal domain is comprised of a homodimeric adenylation domain (AD) and ECTD. The structural and biochemical data demonstrate that Atg8 is initially recognized by the C-terminal tail of ECTD and is then transferred to an AD, where the Atg8 C terminus is attacked by the catalytic cysteine to form a thioester bond. Atg8 is then transferred via a trans mechanism to the Atg3 bound to the NTD of the opposite protomer within a dimer.

PubMed: 22055191
DOI: 10.1016/j.molcel.2011.08.035

実験手法

X-RAY DIFFRACTION (2 Å)