9S9K
S. islandicus CdvB (semi open)
Summary for 9S9K
| Entry DOI | 10.2210/pdb9s9k/pdb |
| Descriptor | Cell division protein CdvB, Vps2 like protein (2 entities in total) |
| Functional Keywords | cell division, archaea, cell cycle |
| Biological source | Saccharolobus islandicus |
| Total number of polymer chains | 2 |
| Total formula weight | 43944.14 |
| Authors | |
| Primary citation | 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 Cited by 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: 41543908DOI: 10.1073/pnas.2525941123 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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