5AZF

Crystal structure of LGG-1 complexed with a WEEL peptide

5AZF の概要

• エントリーDOI: 10.2210/pdb5azf/pdb
• 関連するPDBエントリー: 5AZG 5AZH
• 分子名称: Protein lgg-1, peptide from Autophagy-related protein 19, CADMIUM ION, ... (5 entities in total)
• 機能のキーワード: autophagy, ubiquitin-like, protein binding
• 由来する生物種: Caenorhabditis elegans; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 31267.34

構造登録者

Watanabe, Y.,Noda, N.N. (登録日: 2015-10-05, 公開日: 2015-12-30, 最終更新日: 2023-11-08)

主引用文献

Wu, F.,Watanabe, Y.,Guo, X.Y.,Qi, X.,Wang, P.,Zhao, H.Y.,Wang, Z.,Fujioka, Y.,Zhang, H.,Ren, J.Q.,Fang, T.C.,Shen, Y.X.,Feng, W.,Hu, J.J.,Noda, N.N.,Zhang, H.
Structural Basis of the Differential Function of the Two C. elegans Atg8 Homologs, LGG-1 and LGG-2, in Autophagy.
Mol.Cell, 60:914-929, 2015

PubMed Abstract: Multicellular organisms have multiple homologs of the yeast ATG8 gene, but the differential roles of these homologs in autophagy during development remain largely unknown. Here we investigated structure/function relationships in the two C. elegans Atg8 homologs, LGG-1 and LGG-2. lgg-1 is essential for degradation of protein aggregates, while lgg-2 has cargo-specific and developmental-stage-specific roles in aggregate degradation. Crystallography revealed that the N-terminal tails of LGG-1 and LGG-2 adopt the closed and open form, respectively. LGG-1 and LGG-2 interact differentially with autophagy substrates and Atg proteins, many of which carry a LIR motif. LGG-1 and LGG-2 have structurally distinct substrate binding pockets that prefer different residues in the interacting LIR motif, thus influencing binding specificity. Lipidated LGG-1 and LGG-2 possess distinct membrane tethering and fusion activities, which may result from the N-terminal differences. Our study reveals the differential function of two ATG8 homologs in autophagy during C. elegans development.

PubMed: 26687600
DOI: 10.1016/j.molcel.2015.11.019

実験手法

X-RAY DIFFRACTION (1.6 Å)