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TitleSymmetry disruption commits vault particles to disassembly.
Journal, issue, pagesSci Adv, Vol. 8, Issue 6, Page eabj7795, Year 2022
Publish dateFeb 11, 2022
AuthorsPablo Guerra / María González-Alamos / Aida Llauró / Arnau Casañas / Jordi Querol-Audí / Pedro J de Pablo / Núria Verdaguer /
PubMed AbstractVaults are ubiquitous ribonucleoprotein particles involved in a diversity of cellular processes, with promising applications as nanodevices for delivery of multiple cargos. The vault shell is ...Vaults are ubiquitous ribonucleoprotein particles involved in a diversity of cellular processes, with promising applications as nanodevices for delivery of multiple cargos. The vault shell is assembled by the symmetrical association of multiple copies of the major vault protein that, initially, generates half vaults. The pairwise, anti-parallel association of two half vaults produces whole vaults. Here, using a combination of vault recombinant reconstitution and structural techniques, we characterized the molecular determinants for the vault opening process. This process commences with a relaxation of the vault waist, causing the expansion of the inner cavity. Then, local disengagement of amino-terminal domains at the vault midsection seeds a conformational change that leads to the aperture, facilitating access to the inner cavity where cargo is hosted. These results inform a hitherto uncharacterized step of the vault cycle and will aid current engineering efforts leveraging vault for tailored cargo delivery.
External linksSci Adv / PubMed:35138889 / PubMed Central
MethodsEM (single particle)
Resolution3.8 - 9.8 Å
Structure data

EMDB-13478, PDB-7pkr:
Vault structure in primmed conformation
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-13482, PDB-7pky:
Half-vault structure
Method: EM (single particle) / Resolution: 7.9 Å

EMDB-13483, PDB-7pkz:
Vault structure in committed conformation
Method: EM (single particle) / Resolution: 9.8 Å

Source
  • rattus norvegicus (Norway rat)
KeywordsSTRUCTURAL PROTEIN / Transport

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