A vault ribonucleoprotein particle exhibiting 39-fold dihedral symmetry

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

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)525-531
Number of pages7
JournalActa Crystallographica Section D: Biological Crystallography
Volume64
Issue number5
DOIs
Publication statusPublished - Apr 19 2008
Externally publishedYes

Fingerprint

Vault Ribonucleoprotein Particles
Ribonucleoproteins
R Factors
Telomerase
symmetry
Crystallization
Eukaryota
proteins
Proteins
RNA
eukaryotes
ribose
adenosine diphosphate
Crystals
caps
correlation coefficients
crystallization
coefficients
cells
crystals

Keywords

  • Ribonucleoproteins
  • Vault

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

Cite this

A vault ribonucleoprotein particle exhibiting 39-fold dihedral symmetry. / Kato, Koji; Tanaka, Hideaki; Sumizawa, Tomoyuki; Yoshimura, Masato; Yamashita, Eiki; Iwasaki, Kenji; Tsukihara, Tomitake.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 64, No. 5, 19.04.2008, p. 525-531.

Research output: Contribution to journalArticle

Kato, K, Tanaka, H, Sumizawa, T, Yoshimura, M, Yamashita, E, Iwasaki, K & Tsukihara, T 2008, 'A vault ribonucleoprotein particle exhibiting 39-fold dihedral symmetry', Acta Crystallographica Section D: Biological Crystallography, vol. 64, no. 5, pp. 525-531. https://doi.org/10.1107/S0907444908004277
Kato, Koji ; Tanaka, Hideaki ; Sumizawa, Tomoyuki ; Yoshimura, Masato ; Yamashita, Eiki ; Iwasaki, Kenji ; Tsukihara, Tomitake. / A vault ribonucleoprotein particle exhibiting 39-fold dihedral symmetry. In: Acta Crystallographica Section D: Biological Crystallography. 2008 ; Vol. 64, No. 5. pp. 525-531.
@article{1d3f8a9d3f6f4cf88548e0a06a315ee8,
title = "A vault ribonucleoprotein particle exhibiting 39-fold dihedral symmetry",
abstract = "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 {\AA}, 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.",
keywords = "Ribonucleoproteins, Vault",
author = "Koji Kato and Hideaki Tanaka and Tomoyuki Sumizawa and Masato Yoshimura and Eiki Yamashita and Kenji Iwasaki and Tomitake Tsukihara",
year = "2008",
month = "4",
day = "19",
doi = "10.1107/S0907444908004277",
language = "English",
volume = "64",
pages = "525--531",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "0907-4449",
publisher = "John Wiley and Sons Inc.",
number = "5",

}

TY - JOUR

T1 - A vault ribonucleoprotein particle exhibiting 39-fold dihedral symmetry

AU - Kato, Koji

AU - Tanaka, Hideaki

AU - Sumizawa, Tomoyuki

AU - Yoshimura, Masato

AU - Yamashita, Eiki

AU - Iwasaki, Kenji

AU - Tsukihara, Tomitake

PY - 2008/4/19

Y1 - 2008/4/19

N2 - 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.

AB - 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.

KW - Ribonucleoproteins

KW - Vault

UR - http://www.scopus.com/inward/record.url?scp=43249130948&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=43249130948&partnerID=8YFLogxK

U2 - 10.1107/S0907444908004277

DO - 10.1107/S0907444908004277

M3 - Article

C2 - 18453688

AN - SCOPUS:43249130948

VL - 64

SP - 525

EP - 531

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 0907-4449

IS - 5

ER -