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

FEBS Letters

Yao, Yong-Neng¹  Zhu, Guang²  Zhang, Qing-Shuo¹  Yan, Xian-Zhong²  Wang, En-Duo¹ 

[1] State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, the Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, PR China;Department of Biochemistry, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR, PR China

关键词: Aminoacyl–tRNA synthetase;    tRNA2 Arg;    Arginine;    ATP;    4-fluorotryptophan;    Escherichia coli;    aaRS;    aminoacyl-tRNA synthetase;    ArgRS;    arginyl-tRNA synthetase;    4-F-Trp;    4-fluorotryptophan;    FWT;    4-F-Trp-labeled E. coli ArgRS;    tRNA2 Arg;    transfer RNA isoacceptor for arginine(ACG);   

DOI  :  10.1016/S0014-5793(03)00717-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown