Open AccessA vault ribonucleoprotein particle exhibiting 39‐fold dihedral symmetry
Author(s) -
Kato Koji,
Tanaka Hideaki,
Sumizawa Tomoyuki,
Yoshimura Masato,
Yamashita Eiki,
Iwasaki Kenji,
Tsukihara Tomitake
Publication year - 2008
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444908004277
Subject(s) - vault (architecture) , ribonucleoprotein particle , dihedral angle , ribonucleoprotein , crystallography , rna , physics , chemistry , biology , genetics , structural engineering , gene , molecule , quantum mechanics , hydrogen bond , engineering
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 C 2, 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.