Abstract
Elucidation of the structural basis of tRNA recognition and discrimination is the central motive underlying the crystallographic study of the aminoacyl-tRNA synthetases (aaRS). These enzymes must charge (aminoacylate with their corresponding amino acid) only their cognate tRNAs, discriminating against the myriad of very similar noncognate tRNAs, with the high fidelity necessary to ensure accurate translation of the genetic code. From examination of these interactions as observed in the crystal structure of the E. coli glutaminyl-tRNA synthetase (GlnRS) complexed with its cognate tRNA and ATP, now refined at 2.5Å resolution (Rould et al. 1989, 1991), general principles of RNA recognition by proteins are emerging. In contrast to the transcription regulatory proteins that rely solely on binding affinity to discriminate among DNA sequences, the aaRSs may also use regulation of the catalytic steps — allostery — to discriminate amongst tRNAs. The crystal structure of the G1nRS — tRNAGln — ATP complex suggests testable mechanisms for mediating these allosteric effects.
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Rould, M.A., Steitz, T.A. (1992). Structure of the Glutaminyl-tRNA Synthetase — tRNAGln — ATP Complex. In: Eckstein, F., Lilley, D.M.J. (eds) Nucleic Acids and Molecular Biology. Nucleic Acids and Molecular Biology, vol 6. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-77356-3_13
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DOI: https://doi.org/10.1007/978-3-642-77356-3_13
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