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

Abstract

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
Volume547
Issue number1-3
DOIs
StatePublished - Jul 17 2003

Keywords

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

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Substrate-induced conformational changes in Escherichia coli arginyl-tRNA synthetase observed by <sup>19</sup>F NMR spectroscopy'. Together they form a unique fingerprint.

  • Cite this