8QBW

Cryo-EM structure of Vipp1-deltaH6_aa1-219 helical filament with lattice 3 (Vipp1-deltaH6_L3)

8QBW の概要

• エントリーDOI: 10.2210/pdb8qbw/pdb
• EMDBエントリー: 18322
• 分子名称: Phage shock protein A, PspA (1 entity in total)
• 機能のキーワード: vipp1/im30/escrt-iii, membrane remodeling, cryoelectron microscopy, helical filament structure, lipid binding protein
• 由来する生物種: Nostoc punctiforme
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24502.78

構造登録者

Naskar, S.,Low, H.H. (登録日: 2023-08-25, 公開日: 2024-09-11, 最終更新日: 2025-03-26)

主引用文献

Naskar, S.,Merino, A.,Espadas, J.,Singh, J.,Roux, A.,Colom, A.,Low, H.H.
Mechanism for Vipp1 spiral formation, ring biogenesis, and membrane repair.
Nat.Struct.Mol.Biol., 32:571-584, 2025

PubMed Abstract: The ESCRT-III-like protein Vipp1 couples filament polymerization with membrane remodeling. It assembles planar sheets as well as 3D rings and helical polymers, all implicated in mitigating plastid-associated membrane stress. The architecture of Vipp1 planar sheets and helical polymers remains unknown, as do the geometric changes required to transition between polymeric forms. Here we show how cyanobacterial Vipp1 assembles into morphologically-related sheets and spirals on membranes in vitro. The spirals converge to form a central ring similar to those described in membrane budding. Cryo-EM structures of helical filaments reveal a close geometric relationship between Vipp1 helical and planar lattices. Moreover, the helical structures reveal how filaments twist-a process required for Vipp1, and likely other ESCRT-III filaments, to transition between planar and 3D architectures. Overall, our results provide a molecular model for Vipp1 ring biogenesis and a mechanism for Vipp1 membrane stabilization and repair, with implications for other ESCRT-III systems.

PubMed: 39528797
DOI: 10.1038/s41594-024-01401-8

実験手法

ELECTRON MICROSCOPY (3.67 Å)