A vault ribonucleoprotein particle exhibiting 39-fold dihedral symmetry.
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 angstroms, beta = 124.8 degrees . 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.
Kato
Koji
K
Insutitute for Protein Research, Osaka University, 3-2 Yamada-oka, Suita 565-0871, Japan.
Tanaka
Hideaki
H
Sumizawa
Tomoyuki
T
Yoshimura
Masato
M
Yamashita
Eiki
E
Iwasaki
Kenji
K
Tsukihara
Tomitake
T
D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry; D003460:Crystallization / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D008099:Liver / Q000378:metabolism; D008854:Microscopy, Electron; D008958:Models, Molecular; D011065:Poly(ADP-ribose) Polymerases / Q000737:chemistry; D051381:Rats; D020394:Vault Ribonucleoprotein Particles / Q000737:chemistry* / Q000302:isolation & purification* / Q000648:ultrastructure; D014961:X-Ray Diffraction
D002352:Carrier Proteins; D020394:Vault Ribonucleoprotein Particles; D011065:Poly(ADP-ribose) Polymerases