Crystallization and preliminary X-ray crystallographic analysis of dihydrouridine synthase from Thermus thermophilus and its complex with tRNA

Futao Yu; Yoshikazu Tanaka; Shiho Yamamoto; Akiyoshi Nakamura; Shunsuke Kita; Nagisa Hirano; Isao Tanaka; Min Yao

doi:10.1107/S1744309111012486

Crystallization and preliminary X-ray crystallographic analysis of dihydrouridine synthase from Thermus thermophilus and its complex with tRNA

Futao Yu, Yoshikazu Tanaka, Shiho Yamamoto, Akiyoshi Nakamura, Shunsuke Kita, Nagisa Hirano, Isao Tanaka, Min Yao

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

Dihydrouridine synthase (Dus) is responsible for catalyzing dihydrouridine formation in RNA by the reduction of uridine. To elucidate its RNA-recognition mechanism, Dus from Thermus thermophilus (TthDus) and its complex with tRNA were crystallized. Diffraction data sets were collected from crystals of native and selenomethionine-substituted TthDus to resolutions of 1.70 and 2.30 Å, respectively. These crystals belonged to space group P1. Preliminary X - ray crystallographic analysis showed that two molecules of TthDus were contained in an asymmetric unit. In addition, diffraction data were collected to 3.51 Å resolution from a crystal of selenomethionine-substituted TthDus in complex with tRNA, which belonged to space group P41212. Preliminary structural analysis showed that the asymmetric unit contained two TthDus-tRNA complexes.

Original language	English
Pages (from-to)	685-688
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	67
Issue number	6
DOIs	https://doi.org/10.1107/S1744309111012486
Publication status	Published - 2011 Jun
Externally published	Yes

Keywords

Thermus thermophilus
dihydrouridine synthase
flavin mononucleotide
tRNA

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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10.1107/S1744309111012486

Cite this

Yu, F., Tanaka, Y., Yamamoto, S., Nakamura, A., Kita, S., Hirano, N., Tanaka, I., & Yao, M. (2011). Crystallization and preliminary X-ray crystallographic analysis of dihydrouridine synthase from Thermus thermophilus and its complex with tRNA. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 67(6), 685-688. https://doi.org/10.1107/S1744309111012486

Crystallization and preliminary X-ray crystallographic analysis of dihydrouridine synthase from Thermus thermophilus and its complex with tRNA. / Yu, Futao; Tanaka, Yoshikazu; Yamamoto, Shiho; Nakamura, Akiyoshi; Kita, Shunsuke; Hirano, Nagisa; Tanaka, Isao; Yao, Min.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 67, No. 6, 06.2011, p. 685-688.

Research output: Contribution to journal › Article › peer-review

Yu, F, Tanaka, Y, Yamamoto, S, Nakamura, A, Kita, S, Hirano, N, Tanaka, I & Yao, M 2011, 'Crystallization and preliminary X-ray crystallographic analysis of dihydrouridine synthase from Thermus thermophilus and its complex with tRNA', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 67, no. 6, pp. 685-688. https://doi.org/10.1107/S1744309111012486

Yu, Futao ; Tanaka, Yoshikazu ; Yamamoto, Shiho ; Nakamura, Akiyoshi ; Kita, Shunsuke ; Hirano, Nagisa ; Tanaka, Isao ; Yao, Min. / Crystallization and preliminary X-ray crystallographic analysis of dihydrouridine synthase from Thermus thermophilus and its complex with tRNA. In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2011 ; Vol. 67, No. 6. pp. 685-688.

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abstract = "Dihydrouridine synthase (Dus) is responsible for catalyzing dihydrouridine formation in RNA by the reduction of uridine. To elucidate its RNA-recognition mechanism, Dus from Thermus thermophilus (TthDus) and its complex with tRNA were crystallized. Diffraction data sets were collected from crystals of native and selenomethionine-substituted TthDus to resolutions of 1.70 and 2.30 {\AA}, respectively. These crystals belonged to space group P1. Preliminary X - ray crystallographic analysis showed that two molecules of TthDus were contained in an asymmetric unit. In addition, diffraction data were collected to 3.51 {\AA} resolution from a crystal of selenomethionine-substituted TthDus in complex with tRNA, which belonged to space group P41212. Preliminary structural analysis showed that the asymmetric unit contained two TthDus-tRNA complexes.",

keywords = "Thermus thermophilus, dihydrouridine synthase, flavin mononucleotide, tRNA",

author = "Futao Yu and Yoshikazu Tanaka and Shiho Yamamoto and Akiyoshi Nakamura and Shunsuke Kita and Nagisa Hirano and Isao Tanaka and Min Yao",

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Crystallization and preliminary X-ray crystallographic analysis of dihydrouridine synthase from Thermus thermophilus and its complex with tRNA

Abstract

Keywords

ASJC Scopus subject areas

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