6VZF

Crystal Structure of Atg11 Coiled-Coil 3

6VZF の概要

• エントリーDOI: 10.2210/pdb6vzf/pdb
• 分子名称: Autophagy-related protein 11, SULFATE ION (3 entities in total)
• 機能のキーワード: coiled-coil, autophagy, scaffold, structural protein
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12309.65

構造登録者

Margolis, H.K.,Ragusa, M.J. (登録日: 2020-02-28, 公開日: 2020-09-16, 最終更新日: 2024-03-06)

主引用文献

Margolis, H.K.,Katzenell, S.,Leary, K.A.,Ragusa, M.J.
The Third Coiled Coil Domain of Atg11 Is Required for Shaping Mitophagy Initiation Sites.
J.Mol.Biol., 432:5752-5764, 2020

PubMed Abstract: Selective autophagy is the capture of specific cytosolic contents in double-membrane vesicles that subsequently fuse with the vacuole or lysosome, thereby delivering cargo for degradation. Selective autophagy receptors (SARs) mark the cargo for degradation and, in yeast, recruit Atg11, the scaffolding protein for selective autophagy initiation. The mitochondrial protein Atg32 is the yeast SAR that mediates mitophagy, the selective autophagic capture of mitochondria. Atg11-Atg32 interactions concentrate Atg32 into puncta that are thought to represent sites of mitophagy initiation. However, it is unclear how Atg11 concentrates Atg32 to generate mitophagy initiation sites. We show here that the coiled coil 3 (CC3) domain of Atg11 is required for concentrating Atg32 into puncta. We determined the structure of the majority of the CC3, demonstrating that the CC3 forms a parallel homodimer whose dimer interface is formed by a small number of hydrophobic residues. We further show that the CC3 interface is not required for Atg11 dimerization but is required for shaping Atg32 into functional mitophagy initiation sites and for delivery of mitochondria to the vacuole. Our findings suggest that Atg11 self-interactions help concentrate SARs as a necessary precondition for cargo capture.

PubMed: 32896530
DOI: 10.1016/j.jmb.2020.08.025

実験手法

X-RAY DIFFRACTION (2.03 Å)