4yk8

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4yk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yk8 OCA], [https://pdbe.org/4yk8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yk8 RCSB], [https://www.ebi.ac.uk/pdbsum/4yk8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yk8 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

Structure of the Atg101-Atg13 complex reveals essential roles of Atg101 in autophagy initiation.,Suzuki H, Kaizuka T, Mizushima N, Noda NN Nat Struct Mol Biol. 2015 Jun 1. doi: 10.1038/nsmb.3036. PMID:26030876<ref>PMID:26030876</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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