6ZH3

Cryo-EM structure of ESCRT-III helical Vps24 filaments

Summary for 6ZH3

• Entry DOI: 10.2210/pdb6zh3/pdb
• EMDB information: 11212
• Descriptor: Vacuolar protein-sorting-associated protein 24 (1 entity in total)
• Functional Keywords: filament, helical, membrane remodeling, lipid binding protein
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Total number of polymer chains: 4
• Total formula weight: 106248.70

Authors

Huber, S.T.,Mostafavi, S.,Mortensen, S.A.,Sachse, C. (deposition date: 2020-06-20, release date: 2020-08-26, Last modification date: 2024-05-01)

Primary citation

Huber, S.T.,Mostafavi, S.,Mortensen, S.A.,Sachse, C.
Structure and assembly of ESCRT-III helical Vps24 filaments.
Sci Adv, 6:eaba4897-eaba4897, 2020

PubMed Abstract: ESCRT-III proteins mediate a range of cellular membrane remodeling activities such as multivesicular body biogenesis, cytokinesis, and viral release. Critical to these processes is the assembly of ESCRT-III subunits into polymeric structures. In this study, we determined the cryo-EM structure of a helical assembly of Vps24 at 3.2-Å resolution and found that Vps24 adopts an elongated open conformation. Vps24 forms a domain-swapped dimer extended into protofilaments that associate into a double-stranded apolar filament. We demonstrate that, upon binding negatively charged lipids, Vps24 homopolymer filaments undergo partial disassembly into shorter filament fragments and oligomers. Upon the addition of Vps24, Vps2, and Snf7, liposomes are deformed into neck and tubular structures by an ESCRT-III heteropolymer coat. The filamentous Vps24 homopolymer assembly structure and interaction studies reveal how Vps24 could introduce unique geometric properties to mixed-type ESCRT-III heteropolymers and contribute to the process of membrane scission events.

PubMed: 32875105
DOI: 10.1126/sciadv.aba4897

Experimental method

ELECTRON MICROSCOPY (3.2 Å)