7ABK

Helical structure of PspA

7ABK の概要

• エントリーDOI: 10.2210/pdb7abk/pdb
• EMDBエントリー: 11698
• 分子名称: Chloroplast membrane-associated 30 kD protein (1 entity in total)
• 機能のキーワード: pspa, im30, vipp1, escrt-iii, helical reconstruction, cryo-em, membrane remodeling, lipid binding protein
• 由来する生物種: Synechocystis sp. (strain PCC 6803 / Kazusa)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28260.82

構造登録者

Junglas, B.,Huber, S.T.,Mann, D.,Heidler, T.,Clarke, M.,Schneider, D.,Sachse, C. (登録日: 2020-09-07, 公開日: 2021-08-04, 最終更新日: 2024-07-10)

主引用文献

Junglas, B.,Huber, S.T.,Heidler, T.,Schlosser, L.,Mann, D.,Hennig, R.,Clarke, M.,Hellmann, N.,Schneider, D.,Sachse, C.
PspA adopts an ESCRT-III-like fold and remodels bacterial membranes.
Cell, 184:3674-3688.e18, 2021

PubMed Abstract: PspA is the main effector of the phage shock protein (Psp) system and preserves the bacterial inner membrane integrity and function. Here, we present the 3.6 Å resolution cryoelectron microscopy (cryo-EM) structure of PspA assembled in helical rods. PspA monomers adopt a canonical ESCRT-III fold in an extended open conformation. PspA rods are capable of enclosing lipids and generating positive membrane curvature. Using cryo-EM, we visualized how PspA remodels membrane vesicles into μm-sized structures and how it mediates the formation of internalized vesicular structures. Hotspots of these activities are zones derived from PspA assemblies, serving as lipid transfer platforms and linking previously separated lipid structures. These membrane fusion and fission activities are in line with the described functional properties of bacterial PspA/IM30/LiaH proteins. Our structural and functional analyses reveal that bacterial PspA belongs to the evolutionary ancestry of ESCRT-III proteins involved in membrane remodeling.

PubMed: 34166616
DOI: 10.1016/j.cell.2021.05.042

実験手法

ELECTRON MICROSCOPY (3.6 Å)