PMID:12860413
| Citation |
Yao, YN, Zhang, QS, Yan, XZ, Zhu, G and Wang, ED (2003) Substrate-induced conformational changes in Escherichia coli arginyl-tRNA synthetase observed by 19F NMR spectroscopy. FEBS Lett. 547:197-200 |
|---|---|
| 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 tRNA(Arg) 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. |
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| Keywords |
Anticodon/genetics; Arginine/metabolism; Arginine-tRNA Ligase/chemistry; Arginine-tRNA Ligase/metabolism; Binding Sites; Catalytic Domain; Escherichia coli/enzymology; Magnetic Resonance Spectroscopy/methods; Models, Molecular; Protein Conformation; Protein Structure, Secondary; RNA, Transfer, Arg/metabolism; Substrate Specificity; Tryptophan/analogs & derivatives |
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