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.
Tanaka
Hideaki
H
Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Kato
Koji
K
Yamashita
Eiki
E
Sumizawa
Tomoyuki
T
Zhou
Yong
Y
Yao
Min
M
Iwasaki
Kenji
K
Yoshimura
Masato
M
Tsukihara
Tomitake
T
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D008099:Liver / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D051381:Rats; D020394:Vault Ribonucleoprotein Particles / Q000737:chemistry*; D000099187:Major Vault Protein
D020394:Vault Ribonucleoprotein Particles; D000099187:Major Vault Protein