Crystallization and preliminary X-ray diffraction anaylsis of the LOV1 domains of phototropin 1 and 2 from Arabidopsis thaliana

Masayoshi Nakasako, Michihiro Hirata, Nobutaka Shimizu, Shyuntaro Hosokawa, Daisuke Matsuoka, Toshihiko Oka, Masaki Yamamoto, Satoru Tokutomi

研究成果: Article

1 引用 (Scopus)

抄録

Phototropin is a blue-light receptor protein in plants that is responsible for phototropic responses, stomata opening and photo-induced relocation of chloroplasts. Higher plants such as Arabidopsis thaliana have two isoforms of phototropin: phototropin 1 and phototropin 2. Both isoforms comprise a tandem pair of blue-light-absorbing light-oxygen-voltage domains named LOV1 and LOV2 in the N-terminal half and a serine/threonine kinase domain in the C-terminal half. The LOV1 domain is thought to function as a dimerization site. In the present study, recombinant LOV1 domains of A. thaliana phototropin 1 and phototropin 2 were crystallized. The crystal of the LOV1 domain of phototropin 1 belonged to the orthorhombic space group P212121, with unit-cell parameters a = 61.2, b = 64.9, c = 70.8 Å, and diffracted X-rays to a resolution of 2.1 Å. The crystal of the LOV1 domain of phototropin 2 belonged to space group P21, with unit-cell parameters a = 32.5, b = 66.5, c = 56.7 Å, β = 92.4°, and diffracted X-rays to beyond 2.0 Å resolution. In both crystals, two LOV1 domains occupied the crystallographic asymmetric unit.

元の言語English
ページ(範囲)617-621
ページ数5
ジャーナルActa Crystallographica Section F: Structural Biology and Crystallization Communications
64
発行部数7
DOI
出版物ステータスPublished - 2008

Fingerprint

Phototropins
Crystallization
Arabidopsis
X-Ray Diffraction
crystallization
X ray diffraction
diffraction
x rays
Light
Protein Isoforms
Crystals
X-Rays
chloroplasts
crystals
relocation
Plant Proteins
Protein-Serine-Threonine Kinases
X rays
Dimerization
Chloroplasts

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

これを引用

Crystallization and preliminary X-ray diffraction anaylsis of the LOV1 domains of phototropin 1 and 2 from Arabidopsis thaliana. / Nakasako, Masayoshi; Hirata, Michihiro; Shimizu, Nobutaka; Hosokawa, Shyuntaro; Matsuoka, Daisuke; Oka, Toshihiko; Yamamoto, Masaki; Tokutomi, Satoru.

:: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 巻 64, 番号 7, 2008, p. 617-621.

研究成果: Article

Nakasako, Masayoshi ; Hirata, Michihiro ; Shimizu, Nobutaka ; Hosokawa, Shyuntaro ; Matsuoka, Daisuke ; Oka, Toshihiko ; Yamamoto, Masaki ; Tokutomi, Satoru. / Crystallization and preliminary X-ray diffraction anaylsis of the LOV1 domains of phototropin 1 and 2 from Arabidopsis thaliana. :: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2008 ; 巻 64, 番号 7. pp. 617-621.
@article{d62d39dd405c4d54957859d26abe5ef2,
title = "Crystallization and preliminary X-ray diffraction anaylsis of the LOV1 domains of phototropin 1 and 2 from Arabidopsis thaliana",
abstract = "Phototropin is a blue-light receptor protein in plants that is responsible for phototropic responses, stomata opening and photo-induced relocation of chloroplasts. Higher plants such as Arabidopsis thaliana have two isoforms of phototropin: phototropin 1 and phototropin 2. Both isoforms comprise a tandem pair of blue-light-absorbing light-oxygen-voltage domains named LOV1 and LOV2 in the N-terminal half and a serine/threonine kinase domain in the C-terminal half. The LOV1 domain is thought to function as a dimerization site. In the present study, recombinant LOV1 domains of A. thaliana phototropin 1 and phototropin 2 were crystallized. The crystal of the LOV1 domain of phototropin 1 belonged to the orthorhombic space group P212121, with unit-cell parameters a = 61.2, b = 64.9, c = 70.8 {\AA}, and diffracted X-rays to a resolution of 2.1 {\AA}. The crystal of the LOV1 domain of phototropin 2 belonged to space group P21, with unit-cell parameters a = 32.5, b = 66.5, c = 56.7 {\AA}, β = 92.4°, and diffracted X-rays to beyond 2.0 {\AA} resolution. In both crystals, two LOV1 domains occupied the crystallographic asymmetric unit.",
keywords = "Blue-light receptors, LOV domains, Phototropins",
author = "Masayoshi Nakasako and Michihiro Hirata and Nobutaka Shimizu and Shyuntaro Hosokawa and Daisuke Matsuoka and Toshihiko Oka and Masaki Yamamoto and Satoru Tokutomi",
year = "2008",
doi = "10.1107/S1744309108015534",
language = "English",
volume = "64",
pages = "617--621",
journal = "Acta Crystallographica Section F:Structural Biology Communications",
issn = "1744-3091",
publisher = "John Wiley and Sons Ltd",
number = "7",

}

TY - JOUR

T1 - Crystallization and preliminary X-ray diffraction anaylsis of the LOV1 domains of phototropin 1 and 2 from Arabidopsis thaliana

AU - Nakasako, Masayoshi

AU - Hirata, Michihiro

AU - Shimizu, Nobutaka

AU - Hosokawa, Shyuntaro

AU - Matsuoka, Daisuke

AU - Oka, Toshihiko

AU - Yamamoto, Masaki

AU - Tokutomi, Satoru

PY - 2008

Y1 - 2008

N2 - Phototropin is a blue-light receptor protein in plants that is responsible for phototropic responses, stomata opening and photo-induced relocation of chloroplasts. Higher plants such as Arabidopsis thaliana have two isoforms of phototropin: phototropin 1 and phototropin 2. Both isoforms comprise a tandem pair of blue-light-absorbing light-oxygen-voltage domains named LOV1 and LOV2 in the N-terminal half and a serine/threonine kinase domain in the C-terminal half. The LOV1 domain is thought to function as a dimerization site. In the present study, recombinant LOV1 domains of A. thaliana phototropin 1 and phototropin 2 were crystallized. The crystal of the LOV1 domain of phototropin 1 belonged to the orthorhombic space group P212121, with unit-cell parameters a = 61.2, b = 64.9, c = 70.8 Å, and diffracted X-rays to a resolution of 2.1 Å. The crystal of the LOV1 domain of phototropin 2 belonged to space group P21, with unit-cell parameters a = 32.5, b = 66.5, c = 56.7 Å, β = 92.4°, and diffracted X-rays to beyond 2.0 Å resolution. In both crystals, two LOV1 domains occupied the crystallographic asymmetric unit.

AB - Phototropin is a blue-light receptor protein in plants that is responsible for phototropic responses, stomata opening and photo-induced relocation of chloroplasts. Higher plants such as Arabidopsis thaliana have two isoforms of phototropin: phototropin 1 and phototropin 2. Both isoforms comprise a tandem pair of blue-light-absorbing light-oxygen-voltage domains named LOV1 and LOV2 in the N-terminal half and a serine/threonine kinase domain in the C-terminal half. The LOV1 domain is thought to function as a dimerization site. In the present study, recombinant LOV1 domains of A. thaliana phototropin 1 and phototropin 2 were crystallized. The crystal of the LOV1 domain of phototropin 1 belonged to the orthorhombic space group P212121, with unit-cell parameters a = 61.2, b = 64.9, c = 70.8 Å, and diffracted X-rays to a resolution of 2.1 Å. The crystal of the LOV1 domain of phototropin 2 belonged to space group P21, with unit-cell parameters a = 32.5, b = 66.5, c = 56.7 Å, β = 92.4°, and diffracted X-rays to beyond 2.0 Å resolution. In both crystals, two LOV1 domains occupied the crystallographic asymmetric unit.

KW - Blue-light receptors

KW - LOV domains

KW - Phototropins

UR - http://www.scopus.com/inward/record.url?scp=46949099170&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=46949099170&partnerID=8YFLogxK

U2 - 10.1107/S1744309108015534

DO - 10.1107/S1744309108015534

M3 - Article

C2 - 18607090

AN - SCOPUS:46949099170

VL - 64

SP - 617

EP - 621

JO - Acta Crystallographica Section F:Structural Biology Communications

JF - Acta Crystallographica Section F:Structural Biology Communications

SN - 1744-3091

IS - 7

ER -