Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Molecular structure of the ESCRT-III-based archaeal CdvAB cell division machinery.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 123, Issue 3, Page e2525941123, Year 2026
Publish date	Jan 20, 2026
Authors	Tina Drobnič / Ralf Salzer / Tim Nierhaus / Margaret Ke Xin Jiang / Dom Bellini / Astrid Steindorf / Sonja-Verena Albers / Buzz Baum / Jan Löwe /
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 ...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.
External links	Proc Natl Acad Sci U S A / PubMed:41543908 / PubMed Central
Methods	EM (helical sym.) / X-ray diffraction
Resolution	2.2 - 4.07 Å
Structure data	54673 9s97 EMDB-54673, PDB-9s97: CdvB2 filament - low twist Method: EM (helical sym.) / Resolution: 3.2 Å 54674 9s98 EMDB-54674, PDB-9s98: CdvB2 filament - high twist, class A Method: EM (helical sym.) / Resolution: 3.86 Å 54675 9s99 EMDB-54675, PDB-9s99: CdvB2 filament - high twist, class B Method: EM (helical sym.) / Resolution: 3.98 Å 54678 9s9h EMDB-54678, PDB-9s9h: S. islandicus CdvA filament (cryo-EM) Method: EM (helical sym.) / Resolution: 4.07 Å PDB-9s9g: S. islandicus CdvA filament (X-ray) Method: X-RAY DIFFRACTION / Resolution: 2.85 Å PDB-9s9i: S. islandicus CdvA (non-polymerising mutant) Method: X-RAY DIFFRACTION / Resolution: 2.2 Å PDB-9s9j: S. islandicus CdvB (closed) Method: X-RAY DIFFRACTION / Resolution: 2.7 Å PDB-9s9k: S. islandicus CdvB (semi open) Method: X-RAY DIFFRACTION / Resolution: 2.2 Å
Chemicals	ChemComp-HOH: WATER
Source	sulfolobus acidocaldarius (acidophilic) saccharolobus islandicus (archaea)
Keywords	CELL CYCLE / cell division / ESCRT-III / membrane remodelling / archaea