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TitleStructural flexibility of the human vault particle revealed by high-resolution cryo-EM and molecular dynamics simulations.
Journal, issue, pagesNat Commun, Year 2026
Publish dateMay 2, 2026
AuthorsFabio Lapenta / Karen Palacio-Rodriguez / Sergio Cruz-León / Simone Marrancone / Jana Aupič / Nils Marechal / Alexandre Durand / Dihia Moussaoui / Sonia Covaceuszach / Bhavani Gangupam / Claudia D'Ercole / Cristian Parra / Davide Cotugno / Giulia Tomaino / Paolo Tortora / Ario de Marco / Alberto Cassetta / Alessandra Magistrato / Gerhard Hummer /
PubMed AbstractVaults are massive ribonucleoprotein complexes, highly conserved and abundant in eukaryotic cells, yet with unclear function. Their thin-walled barrel-shape architecture is composed of two ...Vaults are massive ribonucleoprotein complexes, highly conserved and abundant in eukaryotic cells, yet with unclear function. Their thin-walled barrel-shape architecture is composed of two symmetrical, antiparallel half-shells, each containing 39 copies of the major vault protein (MVP). The spacious lumen of the vault suggests a role in cellular transport. Although vaults are thought to undergo conformational changes to facilitate cargo exchange, the molecular basis for their inherent flexibility remains unknown. Here, we integrate cryogenic electron microscopy (cryo-EM) and multi-scale molecular dynamics (MD) simulations to reveal the structural determinants of the human vault particle's flexibility. Cryo-EM identified two high-resolution alternative conformational states: a symmetric and an asymmetric structure, pointing to the vault shell's structural plasticity. MD simulations of these conformations revealed that these structures are flexible and exhibit breathing-like motions, and porous solvent-exposed surfaces. Mutagenesis disrupting persistent MD-identified inter-half contacts reduced full MVP shell assembly, confirming the functional relevance of these flexibility determinants. Together, these findings establish the molecular basis for the human vault particle's conformational plasticity.
External linksNat Commun / PubMed:42069735
MethodsEM (single particle)
Resolution3.09 - 9.89 Å
Structure data

53415

9qw9

EMDB-53415, PDB-9qw9:
Human vault protein - primed conformation
Method: EM (single particle) / Resolution: 3.09 Å

53423

9qwq

EMDB-53423, PDB-9qwq:
Human vault protein - committed conformation
Method: EM (single particle) / Resolution: 4.45 Å

EMDB-53438: Human vault protein - local refinement of the waist - primed conformation
Method: EM (single particle) / Resolution: 3.53 Å

EMDB-53439: Human vault protein - local refinement of the waist - committed conformation
Method: EM (single particle) / Resolution: 6.06 Å

EMDB-53440: 39-mer half of the human vault protein
Method: EM (single particle) / Resolution: 9.89 Å

Source
  • homo sapiens (human)
KeywordsCYTOSOLIC PROTEIN / Vault protein / vault / MVP / TRANSPORT PROTEIN

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