6ZVS

C12 symmetry: Bacterial Vipp1 and PspA are members of the ancient ESCRT-III membrane-remodeling superfamily.

これはPDB形式変換不可エントリーです。

6ZVS の概要

• エントリーDOI: 10.2210/pdb6zvs/pdb
• EMDBエントリー: 11468 11469
• 分子名称: Vipp1 (1 entity in total)
• 機能のキーワード: membrane remodelling, lipid binding protein
• 由来する生物種: Nostoc punctiforme
• タンパク質・核酸の鎖数: 72
• 化学式量合計: 2069673.19

構造登録者

Liu, J.,Tassinari, M.,Souza, D.P.,Naskar, S.,Noel, J.K.,Bohuszewicz, O.,Buck, M.,Williams, T.A.,Baum, B.,Low, H.H. (登録日: 2020-07-27, 公開日: 2021-08-04, 最終更新日: 2022-05-04)

主引用文献

Liu, J.,Tassinari, M.,Souza, D.P.,Naskar, S.,Noel, J.K.,Bohuszewicz, O.,Buck, M.,Williams, T.A.,Baum, B.,Low, H.H.
Bacterial Vipp1 and PspA are members of the ancient ESCRT-III membrane-remodeling superfamily.
Cell, 184:3660-3673.e18, 2021

PubMed Abstract: Membrane remodeling and repair are essential for all cells. Proteins that perform these functions include Vipp1/IM30 in photosynthetic plastids, PspA in bacteria, and ESCRT-III in eukaryotes. Here, using a combination of evolutionary and structural analyses, we show that these protein families are homologous and share a common ancient evolutionary origin that likely predates the last universal common ancestor. This homology is evident in cryo-electron microscopy structures of Vipp1 rings from the cyanobacterium Nostoc punctiforme presented over a range of symmetries. Each ring is assembled from rungs that stack and progressively tilt to form dome-shaped curvature. Assembly is facilitated by hinges in the Vipp1 monomer, similar to those in ESCRT-III proteins, which allow the formation of flexible polymers. Rings have an inner lumen that is able to bind and deform membranes. Collectively, these data suggest conserved mechanistic principles that underlie Vipp1, PspA, and ESCRT-III-dependent membrane remodeling across all domains of life.

PubMed: 34166615
DOI: 10.1016/j.cell.2021.05.041

実験手法

ELECTRON MICROSCOPY (7.2 Å)