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Science 16 January 2009:
Vol. 323. no. 5912, pp. 384 - 388
DOI: 10.1126/science.1164975
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Reports

The Structure of Rat Liver Vault at 3.5 Angstrom Resolution

Hideaki Tanaka,1* Koji Kato,1* Eiki Yamashita,1 Tomoyuki Sumizawa,2 Yong Zhou,3 Min Yao,3 Kenji Iwasaki,1,4 Masato Yoshimura,5 Tomitake Tsukihara1,6{dagger}

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.

1 Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
2 University of Occupational and Environmental Health, 1-1 Iseigaoka, Yahatanishi, Kitakyushu, Fukuoka 807-8555, Japan.
3 Faculty of Advanced Life Sciences, Graduate School of Life Sciences, Hokkaido University, Sapporo, Hokkaido 060-0810, Japan.
4 Bio-multisome Research Team, Structural Physiology Research Group, RIKEN Harima Institute, Mikazuki Sayo, Hyogo 679-5148, Japan.
5 National Synchrotron Radiation Research Center, 101 Hsin-Ann Road, Hsinchu Science Park, Hsinchu 30076, Taiwan.
6 Department of Life Science, University of Hyogo, 3-2-1 Koto, Kamighori, Akoh, Hyogo 678-1297, Japan.

* These authors contributed equally to this work.

{dagger} To whom correspondence should be addressed. E-mail: tsuki{at}protein.osaka-u.ac.jp

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Evolution of Vault RNAs.
P. F. Stadler, J. J.-L. Chen, J. Hackermuller, S. Hoffmann, F. Horn, P. Khaitovich, A. K. Kretzschmar, A. Mosig, S. J. Prohaska, X. Qi, et al. (2009)
Mol. Biol. Evol. 26, 1975-1991
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Science. ISSN 0036-8075 (print), 1095-9203 (online)