Tyr-426 of theEscherichia coliasparaginyl-tRNA synthetase, an amino acid in a C-terminal concerved motif, is involved in ATP binding
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(91)80228-U/fullpdf
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3. A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å
4. Specific Sequence Homology and Three-Dimensional Structure of an Aminoacyl Transfer RNA Synthetase
5. Structure of tyrosyl-tRNA synthetase refined at 2.3 Å resolution
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1. The tRNA A76 Hydroxyl Groups Control Partitioning of the tRNA-dependent Pre- and Post-transfer Editing Pathways in Class I tRNA Synthetase;Journal of Biological Chemistry;2015-05
2. Aminoacyl-tRNA Synthetases: Occurrence, Structure, and Function;tRNA;2014-04-30
3. A Family of RNA-Binding Enzymes;Subcellular Biochemistry;1995
4. FUNCTIONS OF THE GENE-PRODUCTS OF ESCHERICHIA-COLI;MICROBIOL REV;1993
5. Functions of the gene products of Escherichia coli;Microbiological Reviews;1993-12
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