PDBsum entry 5e6o

Protein binding/peptide

PDB id: 5e6o

Contents

Protein chains

117 a.a.

Ligands

TRP-GLU-GLU-LEU ×4

Waters ×470

PDB id:

5e6o

Name:

Protein binding/peptide

Title:

Crystal structure of c. Elegans lgg-2 bound to an aim/lir motif

Structure:

Protein lgg-2. Chain: a, b, c, d. Fragment: unp residues 17-130. Engineered: yes. Trp-glu-glu-leu. Chain: e, f, g, h. Engineered: yes

Source:

Caenorhabditis elegans. Organism_taxid: 6239. Gene: lgg-2, zk593.6. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Scheffersomyces stipitis. Organism_taxid: 4924. Other_details: synthetic peptide

Resolution:

1.80Å R-factor: 0.181 R-free: 0.241

Authors:

X.Qi,J.Q.Ren,F.Wu,H.Zhang,W.Feng

Key ref:

F.Wu et al. (2015). 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. PubMed id: 26687600 DOI: 10.1016/j.molcel.2015.11.019

Date:

10-Oct-15 Release date: 06-Jan-16

Protein chains

Q23536  (LGG2_CAEEL) -  Protein lgg-2 from Caenorhabditis elegans

Seq: 130 a.a.

Struc: 117 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.molcel.2015.11.019

Mol Cell 60:914-929 (2015)

PubMed id: 26687600

Structural Basis of the Differential Function of the Two C. elegans Atg8 Homologs, LGG-1 and LGG-2, in Autophagy.

F.Wu, Y.Watanabe, X.Y.Guo, X.Qi, P.Wang, H.Y.Zhao, Z.Wang, Y.Fujioka, H.Zhang, J.Q.Ren, T.C.Fang, Y.X.Shen, W.Feng, J.J.Hu, N.N.Noda, H.Zhang.

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.