2ZUO: The Structure of RAT Liver Vault at 3.5 Angstrom Resolution

Vaults are among the largest cytoplasmic ribonucleoprotein particles and are found in numerous eukaryotic species. Roles in multidrug resistance and innate immunity have been suggested, but the cellular function remains unclear. We have determined the x-ray structure of rat liver vault at 3.5 angstrom resolution and show that the cage structure consists of a dimer of half-vaults, with each half-vault comprising 39 identical major vault protein (MVP) chains. Each MVP monomer folds into 12 domains: nine structural repeat domains, a shoulder domain, a cap-helix domain, and a cap-ring domain. Interactions between the 42-turn-long cap-helix domains are key to stabilizing the particle. The shoulder domain is structurally similar to a core domain of stomatin, a lipid-raft component in erythrocytes and epithelial cells.
MMDB ID: 99596
PDB Deposition Date: 2008/10/24
Updated in MMDB: 2012/07 
Experimental Method:
x-ray diffraction
Resolution: 3.5  Å
Source Organism:
Similar Structures:
Merged PDB IDs:2ZUO 2ZV4 2ZV5
Asymmetric Unit for 2ZUO: 39-meric
Molecular Components in 2ZUO
Label Count Molecule
Proteins (39 molecules)
Major Vault Protein
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB