5E6N

Crystal structure of C. elegans LGG-2

Summary for 5E6N

• Entry DOI: 10.2210/pdb5e6n/pdb
• Related: 5E6O
• Descriptor: Protein lgg-2 (2 entities in total)
• Functional Keywords: ubiquitin-like protein, atg8 protein family, protein binding
• Biological source: Caenorhabditis elegans
• Cellular location: Cytoplasmic vesicle, autophagosome : Q23536
• Total number of polymer chains: 2
• Total formula weight: 27697.71

Authors

Qi, X.,Ren, J.Q.,Wu, F.,Zhang, H.,Feng, W. (deposition date: 2015-10-10, release date: 2016-01-06, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.102 Å)