9S9G

S. islandicus CdvA filament (X-ray)

9S9G の概要

• エントリーDOI: 10.2210/pdb9s9g/pdb
• 分子名称: Cell division protein CdvA (1 entity in total)
• 機能のキーワード: cell division, archaea, cell cycle
• 由来する生物種: Saccharolobus islandicus
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 380453.88

構造登録者

Salzer, R.,Lowe, J.,Bellini, D. (登録日: 2025-08-06, 公開日: 2026-01-28)

主引用文献

Drobnic, T.,Salzer, R.,Nierhaus, T.,Jiang, M.K.X.,Bellini, D.,Steindorf, A.,Albers, S.V.,Baum, B.,Lowe, J.
Molecular structure of the ESCRT-III-based archaeal CdvAB cell division machinery.
Proc.Natl.Acad.Sci.USA, 123:e2525941123-e2525941123, 2026

PubMed Abstract: Most prokaryotes divide using filaments of the tubulin-like FtsZ protein, while some archaea employ instead ESCRT-III-like proteins and their filaments for cell division and cytokinesis. The alternative archaeal system comprises Cdv proteins and is thought to bear some resemblance to ESCRT-III-based membrane remodeling in other domains of life, including eukaryotes, especially during abscission. Here, we present biochemical, crystallographic, and cryo-EM studies of the Cdv machinery. CdvA, an early non-ESCRT component, adopts a PRC-domain/coiled-coil fold and polymerizes into long double-stranded helical filaments, mainly via hydrophobic interfaces. Monomeric CdvB adopts the canonical ESCRT-III fold in both a closed and a distinct "semiopen" conformation. Soluble CdvB2 filaments are composed of subunits in the closed state, appearing to transition to the open, active state only when polymerized on membranes. Short N-terminal amphipathic helices in all CdvB paralogues, B, B1, and B2, mediate membrane binding and are required for liposome recruitment in vitro. We provide a molecular overview of archaeal ESCRT-III-based cytokinesis machinery, the definitive demonstration that CdvB proteins are bona fide ESCRT-III homologues, and reveal the molecular basis for membrane engagement. Thus, we illuminate conserved principles of ESCRT-mediated membrane remodeling and extend them to an anciently diverged archaeal lineage.

PubMed: 41543908
DOI: 10.1073/pnas.2525941123

実験手法

X-RAY DIFFRACTION (2.85 Å)