Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Escherichia coli in complex with the acceptor-TC domain of tRNA

Kosuke Ito, Hao Qi, Yoshihiro Shimizu, Ryo Murakami, Kin Ichiro Miura, Takuya Ueda, Toshio Uchiumi

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Peptidyl-tRNA hydrolase (Pth) cleaves the ester bond between the peptide and the tRNA of peptidyl-tRNA molecules, which are the product of aborted translation. In the present work, Pth from Escherichia coli was crystallized with the acceptor-TC domain of tRNA using 1,4-butanediol as a precipitant. The crystals belonged to the hexagonal space group P61, with unit-cell parameters a = b = 55.1, c = 413.1 Å, and diffracted X-rays beyond 2.4 Å resolution. The asymmetric unit is expected to contain two complexes of Pth and the acceptor-TC domain of tRNA (V M = 2.8 Å 3 Da -1), with a solvent content of 60.8%. The structure is being solved by molecular replacement.

Original languageEnglish
Pages (from-to)1566-1569
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
Issue number12
DOIs
Publication statusPublished - 2011 Dec 1
Externally publishedYes

Fingerprint

X ray analysis
Escherichia
Transfer RNA
Crystallization
Escherichia coli
X-Rays
crystallization
peptides
esters
x rays
Esters
products
cells
crystals
molecules
X rays
Peptides
Crystals
Molecules
aminoacyl-tRNA hydrolase

Keywords

  • acceptor-TC domain
  • peptidyl-tRNA hydrolases

ASJC Scopus subject areas

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

Cite this

Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Escherichia coli in complex with the acceptor-TC domain of tRNA. / Ito, Kosuke; Qi, Hao; Shimizu, Yoshihiro; Murakami, Ryo; Miura, Kin Ichiro; Ueda, Takuya; Uchiumi, Toshio.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 67, No. 12, 01.12.2011, p. 1566-1569.

Research output: Contribution to journalArticle

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