Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Thermus thermophilus HB8

Ami Matsumoto; Yoshihiro Shimizu; Chie Takemoto; Takuya Ueda; Toshio Uchiumi; Kosuke Ito

doi:10.1107/S1744309113003424

Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Thermus thermophilus HB8

Ami Matsumoto, Yoshihiro Shimizu, Chie Takemoto, Takuya Ueda, Toshio Uchiumi, Kosuke Ito^*

^*Corresponding author for this work

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

1 Citation (Scopus)

Abstract

Peptidyl-tRNA is produced from the ribosome as a result of aborted translation. Peptidyl-tRNA hydrolase cleaves the ester bond between the peptide and the tRNA of peptidyl-tRNA molecules, to recycle tRNA for further rounds of protein synthesis. In this study, peptidyl-tRNA hydrolase from Thermus thermophilus HB8 (TthPth) was crystallized using 2-methyl-2,4-pentanediol as a precipitant. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 47.45, b = 53.92, c = 58.67Å, and diffracted X-rays to atomic resolution (beyond 1.0Å resolution). The asymmetric unit is expected to contain one TthPth molecule, with a solvent content of 27.13% (V M = 1.69Å³Da^-1). The structure is being solved by molecular replacement.

Original language	English
Pages (from-to)	332-335
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	69
Issue number	3
DOIs	https://doi.org/10.1107/S1744309113003424
Publication status	Published - 2013 Mar
Externally published	Yes

Keywords

Thermus thermophilus
peptidyl-tRNA hydrolase

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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10.1107/S1744309113003424

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title = "Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Thermus thermophilus HB8",

abstract = "Peptidyl-tRNA is produced from the ribosome as a result of aborted translation. Peptidyl-tRNA hydrolase cleaves the ester bond between the peptide and the tRNA of peptidyl-tRNA molecules, to recycle tRNA for further rounds of protein synthesis. In this study, peptidyl-tRNA hydrolase from Thermus thermophilus HB8 (TthPth) was crystallized using 2-methyl-2,4-pentanediol as a precipitant. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 47.45, b = 53.92, c = 58.67{\AA}, and diffracted X-rays to atomic resolution (beyond 1.0{\AA} resolution). The asymmetric unit is expected to contain one TthPth molecule, with a solvent content of 27.13% (V M = 1.69{\AA}3Da-1). The structure is being solved by molecular replacement.",

keywords = "Thermus thermophilus, peptidyl-tRNA hydrolase",

author = "Ami Matsumoto and Yoshihiro Shimizu and Chie Takemoto and Takuya Ueda and Toshio Uchiumi and Kosuke Ito",

year = "2013",

month = mar,

doi = "10.1107/S1744309113003424",

language = "English",

volume = "69",

pages = "332--335",

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T1 - Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Thermus thermophilus HB8

AU - Matsumoto, Ami

AU - Shimizu, Yoshihiro

AU - Takemoto, Chie

AU - Ueda, Takuya

AU - Uchiumi, Toshio

AU - Ito, Kosuke

PY - 2013/3

Y1 - 2013/3

N2 - Peptidyl-tRNA is produced from the ribosome as a result of aborted translation. Peptidyl-tRNA hydrolase cleaves the ester bond between the peptide and the tRNA of peptidyl-tRNA molecules, to recycle tRNA for further rounds of protein synthesis. In this study, peptidyl-tRNA hydrolase from Thermus thermophilus HB8 (TthPth) was crystallized using 2-methyl-2,4-pentanediol as a precipitant. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 47.45, b = 53.92, c = 58.67Å, and diffracted X-rays to atomic resolution (beyond 1.0Å resolution). The asymmetric unit is expected to contain one TthPth molecule, with a solvent content of 27.13% (V M = 1.69Å3Da-1). The structure is being solved by molecular replacement.

AB - Peptidyl-tRNA is produced from the ribosome as a result of aborted translation. Peptidyl-tRNA hydrolase cleaves the ester bond between the peptide and the tRNA of peptidyl-tRNA molecules, to recycle tRNA for further rounds of protein synthesis. In this study, peptidyl-tRNA hydrolase from Thermus thermophilus HB8 (TthPth) was crystallized using 2-methyl-2,4-pentanediol as a precipitant. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 47.45, b = 53.92, c = 58.67Å, and diffracted X-rays to atomic resolution (beyond 1.0Å resolution). The asymmetric unit is expected to contain one TthPth molecule, with a solvent content of 27.13% (V M = 1.69Å3Da-1). The structure is being solved by molecular replacement.

KW - Thermus thermophilus

KW - peptidyl-tRNA hydrolase

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JO - Acta Crystallographica Section F:Structural Biology Communications

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SN - 1744-3091

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ER -

Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Thermus thermophilus HB8

Abstract

Keywords

ASJC Scopus subject areas

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