4V60

The structure of rat liver vault at 3.5 angstrom resolution

This is a non-PDB format compatible entry.

Summary for 4V60

• Entry DOI: 10.2210/pdb4v60/pdb
• Related: 2ZV4 2ZV5
• Descriptor: Major vault protein (1 entity in total)
• Functional Keywords: 9 repeat domains, protein-protein complex, ribonucleoprotein, structural protein
• Biological source: Rattus norvegicus (rat)
• Cellular location: Cytoplasm: Q62667
• Total number of polymer chains: 39
• Total formula weight: 3740884.25

Authors

Kato, K.,Zhou, Y.,Tanaka, H.,Yao, M.,Yamashita, E.,Yoshimura, M.,Tsukihara, T. (deposition date: 2008-10-24, release date: 2014-07-09, Last modification date: 2024-04-03)

Primary citation

Tanaka, H.,Kato, K.,Yamashita, E.,Sumizawa, T.,Zhou, Y.,Yao, M.,Iwasaki, K.,Yoshimura, M.,Tsukihara, T.
The structure of rat liver vault at 3.5 angstrom resolution
Science, 323:384-388, 2009

PubMed Abstract: 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.

PubMed: 19150846
DOI: 10.1126/science.1164975

Experimental method

X-RAY DIFFRACTION (3.5 Å)