Conserved amino acids near the carboxy terminus of bacterial tyrosyl-tRNA synthetase are involved in tRNA and Tyr-AMP binding
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(01)02214-1/fullpdf
Reference24 articles.
1. Aminoacyl-tRNA Synthesis
2. Recognition of tRNATyr by tyrosyl-tRNA synthetase
3. Discrimination between transfer-RNAs by tyrosyl-tRNA synthetase
4. Structure of tyrosyl-tRNA synthetase refined at 2.3 Å resolution
5. Deletion mutagenesis using an ‘M13 splint’: the N-terminal structural domain of tyrosyl-tRNA synthetase (B. stearothermophilus) catalyses the formation of tyrosyl adenylate.
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1. Two Forms of Tyrosyl-tRNA Synthetase from Pseudomonas aeruginosa: Characterization and Discovery of Inhibitory Compounds;SLAS DISCOVERY: Advancing the Science of Drug Discovery;2020-06-25
2. Structural basis for recognition of cognate tRNA by tyrosyl-tRNA synthetase from three kingdoms;Nucleic Acids Research;2007-06-18
3. Regulation of a glutamyl-tRNA synthetase by the heme status;Proceedings of the National Academy of Sciences;2007-02-20
4. Evolution of the tRNATyr/TyrRS aminoacylation systems;Biochimie;2005-09
5. Toward the Full Set of Human Mitochondrial Aminoacyl-tRNA Synthetases: Characterization of AspRS and TyrRS;Biochemistry;2005-03-01
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