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Amino Acids

, Volume 32, Issue 4, pp 479–482 | Cite as

Crystallization and preliminary X-ray diffraction analysis of E. coli arginyl-tRNA synthetase in complex form with a tRNAArg

  • M. Zhou
  • A. Azzi
  • X. Xia
  • E.-D. Wang
  • S.-X. Lin
Article

Summary.

Amino acids are building blocks of proteins, while aminoacyl-tRNA synthetases (aaRSs) catalyze the first reaction in such building: the biosynthesis of proteins. The E. coli arginyl-tRNA synthetase (ArgRS) has been crystallized in complex form with tRNAArg (B. stearothermophilus), at pH 5.6 using ammonium sulfate as a precipitating agent. Two crystal forms have been identified based on unit cell dimension. The complete data sets from both crystal forms have been collected with a primitive hexagonal space group. A data set of Form II crystals at 3.2 Å and 94% completeness has been obtained, with unit cell parameters a = b = 98.0 Å, c = 463.2 Å, and α = β = 90°, γ = 120°, being different from a = b = 110.8 Å, c = 377.8 Å for form I. The structure determination will demonstrate the interaction of these two macromolecules to understand the special mechanism of ArgRS that requires the presence of tRNA for amino acid activation. Such complex structure also provides a wide opening for inhibitor search using bioinformatics.

Keywords: Amino acids – Arginyl-tRNA synthetase – tRNAArg – Protein-RNA complex – Macromolecular crystallization – Amino acid activation – Aminoacylation – Protein biosynthesis 

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Copyright information

© Springer-Verlag 2006

Authors and Affiliations

  • M. Zhou
    • 1
  • A. Azzi
    • 1
  • X. Xia
    • 2
  • E.-D. Wang
    • 2
  • S.-X. Lin
    • 1
    • 3
  1. 1.Laboratory of Molecular EndocrinologyCHUL Research Center and Laval UniversityQuébecCanada
  2. 2.State Key Laboratory of Molecular BiologyShanghai Institute of Biochemistry and Cell Biology (SIBCB), Shanghai Institutes of Biological Sciences (SIBS)ShanghaiChina
  3. 3.Laboratory for Exchange Visitors and Structural Biology Platform, SIBCB, SIBSShanghaiChina

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