6BP8

Recombinant major vault protein [Rattus norvegicus] structure in solution: conformation 1

Summary for 6BP8

• Entry DOI: 10.2210/pdb6bp8/pdb
• Related: 6BP7
• EMDB information: 7125 7126
• Descriptor: Major vault protein (1 entity in total)
• Functional Keywords: vault recombinant protein structure engineered nano-particle, structural protein
• Biological source: Rattus norvegicus (Rat)
• Total number of polymer chains: 1
• Total formula weight: 103931.30

Authors

Ding, K.,Zhang, X.,Mrazek, J.,Kickhoefer, V.A.,Lai, M.,Ng, H.L.,Yang, O.O.,Rome, L.H.,Zhou, Z.H. (deposition date: 2017-11-22, release date: 2018-04-04, Last modification date: 2025-05-14)

Primary citation

Ding, K.,Zhang, X.,Mrazek, J.,Kickhoefer, V.A.,Lai, M.,Ng, H.L.,Yang, O.O.,Rome, L.H.,Zhou, Z.H.
Solution Structures of Engineered Vault Particles.
Structure, 26:619-626.e3, 2018

PubMed 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.

PubMed: 29551289
DOI: 10.1016/j.str.2018.02.014

Experimental method

ELECTRON MICROSCOPY (4.9 Å)