4GDK

Crystal Structure of Human Atg12~Atg5 Conjugate in Complex with an N-terminal Fragment of Atg16L1

4GDK の概要

• エントリーDOI: 10.2210/pdb4gdk/pdb
• 関連するPDBエントリー: 4GDL
• 分子名称: Ubiquitin-like protein ATG12, Autophagy protein 5, Autophagy-related protein 16-1, ... (5 entities in total)
• 機能のキーワード: protein-protein conjugate, protein-protein complex, ubiquitin-like protein, autophagy, e3 ligase, ubiquitin-like fold, structural protein, isopeptide bond, cytoplasm and autophagosomal membranes, protein binding
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm : O94817 Q9H1Y0 Q676U5
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 94903.30

構造登録者

Otomo, C.,Metlagel, Z.,Takaesu, G.,Otomo, T. (登録日: 2012-07-31, 公開日: 2012-12-05, 最終更新日: 2024-11-20)

主引用文献

Otomo, C.,Metlagel, Z.,Takaesu, G.,Otomo, T.
Structure of the human ATG12~ATG5 conjugate required for LC3 lipidation in autophagy.
Nat.Struct.Mol.Biol., 20:59-66, 2013

PubMed Abstract: The autophagy factor ATG12~ATG5 conjugate exhibits E3 ligase-like activity which facilitates the lipidation of members of the LC3 family. The crystal structure of the human ATG12~ATG5 conjugate bound to the N-terminal region of ATG16L1, the factor that recruits the conjugate to autophagosomal membranes, reveals an integrated architecture in which ATG12 docks onto ATG5 through conserved residues. ATG12 and ATG5 are oriented such that other conserved residues on each molecule, including the conjugation junction, form a continuous surface patch. Mutagenesis data support the importance of both the interface between ATG12 and ATG5 and the continuous patch for E3 activity. The ATG12~ATG5 conjugate interacts with the E2 enzyme ATG3 with high affinity through another surface location that is exclusive to ATG12, suggesting a different role of the continuous patch in E3 activity. These findings provide a foundation for understanding the mechanism of LC3 lipidation.

PubMed: 23202584
DOI: 10.1038/nsmb.2431

実験手法

X-RAY DIFFRACTION (2.7 Å)