Science Advances

Supplementary Materials

This PDF file includes:

  • fig. S1. Vps4 oligomerizes into a hexamer in the presence of ATP.
  • fig. S2. Cryo-EM images of Vps4 oligomer.
  • fig. S3. Flow chart of particle classification and 3D map reconstruction.
  • fig. S4. Map resolution estimation and projection angle distribution.
  • fig. S5. Fitting of the Vps4 hexamer structure into the cryo-EM map.
  • fig. S6. Molecular dynamics flexible fitting.
  • fig. S7. Comparison of the crystal structure and Vps4 hexamer subunit structures.
  • fig. S8. Sequence alignments of Vps4 proteins from S. cerevisiae, Schizosaccharomyces pombe, Caenorhabditis elegans, Drosophila melanogaster, and Homo sapiens.
  • fig. S9. Residues at subunit interface III are important for Vps4 oligomerization and ATPase activity.
  • fig. S10. Structural comparison of Vps4 subunits in the open and closed conformations.
  • fig. S11. One wild-type subunit per hexamer is sufficient to maintain full Vps4 hexamer ATPase activity.
  • fig. S12. Filament disassembly activity of Vps4.

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Other Supplementary Material for this manuscript includes the following:

  • movie S1(.mov format). Molecular dynamic flexible fitting into Vps4 open and closed cryo-EM maps.
  • movie S2 (.mov format). Morphing motion between Vps4 open and closed models.

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