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A vault ribonucleoprotein particle exhibiting 39-fold dihedral symmetry

2008; Wiley; Volume: 64; Issue: 5 Linguagem: Inglês

10.1107/s0907444908004277

1399-0047

Koji Kato, Hideaki Tanaka, Tomoyuki Sumizawa, Masato Yoshimura, Eiki Yamashita, Kenji Iwasaki, Tomitake Tsukihara,

RNA modifications and cancer

Vault is a 12.9 MDa ribonucleoprotein particle with a barrel-like shape, two protruding caps and an invaginated waist structure that is highly conserved in a wide variety of eukaryotes. Multimerization of the major vault protein (MVP) is sufficient to assemble the entire exterior shell of the barrel-shaped vault particle. Multiple copies of two additional proteins, vault poly(ADP-ribose) polymerase (VPARP) and telomerase-associated protein 1 (TEP1), as well as a small vault RNA (vRNA), are also associated with vault. Here, the crystallization of vault particles is reported. The crystals belong to space group C2, with unit-cell parameters a = 708.0, b = 385.0, c = 602.9 Å, β = 124.8°. Rotational symmetry searches based on the R factor and correlation coefficient from noncrystallographic symmetry (NCS) averaging indicated that the particle has 39-fold dihedral symmetry.