4hpq

</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=4hpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hpq OCA], [https://pdbe.org/4hpq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hpq RCSB], [https://www.ebi.ac.uk/pdbsum/4hpq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hpq ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Macroautophagy is a bulk clearance mechanism in which the double-membraned phagophore grows and engulfs cytosolic material. In yeast, the phagophore nucleates from a cluster of 20-30 nm diameter Atg9-containing vesicles located at a multiprotein assembly known as the preautophagosomal structure (PAS). The crystal structure of a 2:2:2 complex of the earliest acting PAS proteins, Atg17, Atg29, and Atg31, was solved at 3.05 A resolution. Atg17 is crescent shaped with a 10 nm radius of curvature. Dimerization of the Atg17-Atg31-Atg29 complex is critical for both PAS formation and autophagy, and each dimer contains two separate and complete crescents. Upon induction of autophagy, Atg17-Atg31-Atg29 assembles with Atg1 and Atg13, which in turn initiates the formation of the phagophore. The C-terminal EAT domain of Atg1 was shown to sense membrane curvature, dimerize, and tether lipid vesicles. These data suggest a structural mechanism for the organization of Atg9 vesicles into the early phagophore.

Architecture of the atg17 complex as a scaffold for autophagosome biogenesis.,Ragusa MJ, Stanley RE, Hurley JH Cell. 2012 Dec 21;151(7):1501-12. doi: 10.1016/j.cell.2012.11.028. Epub 2012 Dec , 6. PMID:23219485<ref>PMID:23219485</ref>

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

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== References ==

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