4HPQ

Crystal Structure of the Atg17-Atg31-Atg29 Complex

Summary for 4HPQ

• Entry DOI: 10.2210/pdb4hpq/pdb
• Descriptor: Atg29, Atg31, Atg17 (3 entities in total)
• Functional Keywords: autophagy, protein transport
• Biological source: Lachancea thermotolerans CBS 6340 (yeast); More
• Total number of polymer chains: 6
• Total formula weight: 147646.86

Authors

Stanley, R.E.,Ragusa, M.J.,Hurley, J.H. (deposition date: 2012-10-24, release date: 2012-12-26, Last modification date: 2024-02-28)

Primary citation

Ragusa, M.J.,Stanley, R.E.,Hurley, J.H.
Architecture of the atg17 complex as a scaffold for autophagosome biogenesis.
Cell(Cambridge,Mass.), 151:1501-1512, 2012

PubMed Abstract: 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 Å 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.

PubMed: 23219485
DOI: 10.1016/j.cell.2012.11.028

Experimental method

X-RAY DIFFRACTION (3.06 Å)