7PKR

Vault structure in primmed conformation

This is a non-PDB format compatible entry.

Summary for 7PKR

• Entry DOI: 10.2210/pdb7pkr/pdb
• EMDB information: 13478
• Descriptor: Major vault protein (1 entity in total)
• Functional Keywords: transport, structural protein
• Biological source: Rattus norvegicus (Rat)
• Total number of polymer chains: 78
• Total formula weight: 7481768.50

Authors

Guerra, P.,Gonzalez-Alamos, M.,Llauro, A.,Casanas, A.,Querol-Audi, J.,de Pablo, P.,Verdaguer, N. (deposition date: 2021-08-26, release date: 2022-03-16, Last modification date: 2024-07-17)

Primary citation

Guerra, P.,Gonzalez-Alamos, M.,Llauro, A.,Casanas, A.,Querol-Audi, J.,de Pablo, P.J.,Verdaguer, N.
Symmetry disruption commits vault particles to disassembly.
Sci Adv, 8:eabj7795-eabj7795, 2022

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 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.

PubMed: 35138889
DOI: 10.1126/sciadv.abj7795

Experimental method

ELECTRON MICROSCOPY (3.8 Å)