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-Structure paper
Title | Symmetry disruption commits vault particles to disassembly. |
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Journal, issue, pages | Sci Adv, Vol. 8, Issue 6, Page eabj7795, Year 2022 |
Publish date | Feb 11, 2022 |
Authors | Pablo Guerra / María González-Alamos / Aida Llauró / Arnau Casañas / Jordi Querol-Audí / Pedro J de Pablo / Núria Verdaguer / |
PubMed Abstract | 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 ...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 links | Sci Adv / PubMed:35138889 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.8 - 9.8 Å |
Structure data | EMDB-13478, PDB-7pkr: EMDB-13482, PDB-7pky: EMDB-13483, PDB-7pkz: |
Source |
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Keywords | STRUCTURAL PROTEIN / Transport |