4HPQ

Crystal Structure of the Atg17-Atg31-Atg29 Complex

4HPQ の概要

• エントリーDOI: 10.2210/pdb4hpq/pdb
• 分子名称: Atg29, Atg31, Atg17 (3 entities in total)
• 機能のキーワード: autophagy, protein transport
• 由来する生物種: Lachancea thermotolerans CBS 6340 (yeast); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 147646.86

構造登録者

Stanley, R.E.,Ragusa, M.J.,Hurley, J.H. (登録日: 2012-10-24, 公開日: 2012-12-26, 最終更新日: 2024-02-28)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.06 Å)