4P1N

Crystal structure of Atg1-Atg13 complex

Summary for 4P1N

• Entry DOI: 10.2210/pdb4p1n/pdb
• Related: 4P1W
• Descriptor: Atg1 tMIT, Atg13 MIM (3 entities in total)
• Functional Keywords: complex, protein transport
• Biological source: Kluyveromyces marxianus; More
• Total number of polymer chains: 4
• Total formula weight: 75989.83

Authors

Fujioka, Y.,Noda, N.N. (deposition date: 2014-02-27, release date: 2014-05-07, Last modification date: 2023-12-27)

Primary citation

Fujioka, Y.,Suzuki, S.W.,Yamamoto, H.,Kondo-Kakuta, C.,Kimura, Y.,Hirano, H.,Akada, R.,Inagaki, F.,Ohsumi, Y.,Noda, N.N.
Structural basis of starvation-induced assembly of the autophagy initiation complex.
Nat.Struct.Mol.Biol., 21:513-521, 2014

PubMed Abstract: Assembly of the preautophagosomal structure (PAS) is essential for autophagy initiation in yeast. Starvation-induced dephosphorylation of Atg13 is required for the formation of the Atg1-Atg13-Atg17-Atg29-Atg31 complex (Atg1 complex), a prerequisite for PAS assembly. However, molecular details underlying these events have not been established. Here we studied the interactions of yeast Atg13 with Atg1 and Atg17 by X-ray crystallography. Atg13 binds tandem microtubule interacting and transport domains in Atg1, using an elongated helix-loop-helix region. Atg13 also binds Atg17, using a short region, thereby bridging Atg1 and Atg17 and leading to Atg1-complex formation. Dephosphorylation of specific serines in Atg13 enhanced its interaction with not only Atg1 but also Atg17. These observations update the autophagy-initiation model as follows: upon starvation, dephosphorylated Atg13 binds both Atg1 and Atg17, and this promotes PAS assembly and autophagy progression.

PubMed: 24793651
DOI: 10.1038/nsmb.2822

Experimental method

X-RAY DIFFRACTION (2.2 Å)