4YK8
Crystal structure of the Atg101-Atg13 complex from fission yeast
Summary for 4YK8
| Entry DOI | 10.2210/pdb4yk8/pdb |
| Descriptor | Meiotically up-regulated gene 66 protein, Autophagy protein 13 (2 entities in total) |
| Functional Keywords | autophagy, horma, protein transport |
| Biological source | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) More |
| Total number of polymer chains | 2 |
| Total formula weight | 47880.88 |
| Authors | Suzuki, H.,Noda, N.N. (deposition date: 2015-03-04, release date: 2015-06-03, Last modification date: 2024-03-20) |
| Primary citation | Suzuki, H.,Kaizuka, T.,Mizushima, N.,Noda, N.N. Structure of the Atg101-Atg13 complex reveals essential roles of Atg101 in autophagy initiation. Nat.Struct.Mol.Biol., 22:572-580, 2015 Cited by PubMed Abstract: Atg101 is an essential component of the autophagy-initiating ULK complex in higher eukaryotes, but it is absent from the functionally equivalent Atg1 complex in budding yeast. Here, we report the crystal structure of the fission yeast Atg101-Atg13 complex. Atg101 has a Hop1, Rev7 and Mad2 (HORMA) architecture similar to that of Atg13. Mad2 HORMA has two distinct conformations (O-Mad2 and C-Mad2), and, intriguingly, Atg101 resembles O-Mad2 rather than the C-Mad2-like Atg13. Atg13 HORMA from higher eukaryotes possesses an inherently unstable fold, which is stabilized by Atg101 via interactions analogous to those between O-Mad2 and C-Mad2. Mutational studies revealed that Atg101 is responsible for recruiting downstream factors to the autophagosome-formation site in mammals via a newly identified WF finger. These data define the molecular functions of Atg101, providing a basis for elucidating the molecular mechanisms of mammalian autophagy initiation by the ULK complex. PubMed: 26030876DOI: 10.1038/nsmb.3036 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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