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Solution Structures of Engineered Vault Particles.


ABSTRACT: Prior crystal structures of the vault have provided clues of its structural variability but are non-conclusive due to crystal packing. Here, we obtained vaults by engineering at the N terminus of rat major vault protein (MVP) an HIV-1 Gag protein segment and determined their near-atomic resolution (?4.8 Å) structures in a solution/non-crystalline environment. The barrel-shaped vaults in solution adopt two conformations, 1 and 2, both with D39 symmetry. From the N to C termini, each MVP monomer has three regions: body, shoulder, and cap. While conformation 1 is identical to one of the crystal structures, the shoulder in conformation 2 is translocated longitudinally up to 10 Å, resulting in an outward-projected cap. Our structures clarify the structural discrepancies in the body region in the prior crystallography models. The vault's drug-delivery potential is highlighted by the internal disposition and structural flexibility of its Gag-loaded N-terminal extension at the barrel waist of the engineered vault.

SUBMITTER: Ding K 

PROVIDER: S-EPMC5906032 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature

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Solution Structures of Engineered Vault Particles.

Ding Ke K   Zhang Xing X   Mrazek Jan J   Kickhoefer Valerie A VA   Lai Mason M   Ng Hwee L HL   Yang Otto O OO   Rome Leonard H LH   Zhou Z Hong ZH  

Structure (London, England : 1993) 20180315 4


Prior crystal structures of the vault have provided clues of its structural variability but are non-conclusive due to crystal packing. Here, we obtained vaults by engineering at the N terminus of rat major vault protein (MVP) an HIV-1 Gag protein segment and determined their near-atomic resolution (∼4.8 Å) structures in a solution/non-crystalline environment. The barrel-shaped vaults in solution adopt two conformations, 1 and 2, both with D39 symmetry. From the N to C termini, each MVP monomer h  ...[more]

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