Substrate-induced conformational changes in Escherichia coli arginyl-tRNA synthetase observed by 19F NMR spectroscopy

Yong Neng Yao, Qing-Shuo Zhang, Xian Zhong Yan, Guang Zhu, En Duo Wang

Research output: Contribution to journalArticle

7 Scopus citations


The 19F nuclear magnetic resonance (NMR) spectra of 4-fluorotryptophan (4-F-Trp)-labeled Escherichia coli arginyl-tRNA synthetase (ArgRS) show that there are distinct conformational changes in the catalytic core and tRNA anticodon stem and loop-binding domain of the enzyme, when arginine and tRNAArg are added to the unliganded enzyme. We have assigned five fluorine resonances of 4-F-Trp residues (162, 172, 228, 349 and 446) in the spectrum of the fluorinated enzyme by site-directed mutagenesis. The local conformational changes of E. coli ArgRS induced by its substrates observed herein by 19F NMR are similar to those of crystalline yeast homologous enzyme.

Original languageEnglish (US)
Pages (from-to)197-200
Number of pages4
JournalFEBS Letters
Issue number1-3
Publication statusPublished - Jul 17 2003
Externally publishedYes



  • 4-fluorotryptophan
  • Aminoacyl-tRNA synthetase
  • Arginine
  • ATP
  • Escherichia coli
  • TRNA

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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