ArticleThe EMBO journal2002
Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.
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96 citing papers in PubMed, 190 citations in OpenAlex.
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- The binding mode of orphan glycyl-tRNA synthetase with tRNA supports the synthetase classification and reveals large domain movements.Science advances · 2023Article
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- The recurrent missense mutation p.(Arg367Trp) in YARS1 causes a distinct neurodevelopmental phenotype.Journal of molecular medicine (Berlin, Germany) · 2021Review
- The Coenzyme A Level Modulator Hopantenate (HoPan) Inhibits Phosphopantotenoylcysteine Synthetase Activity.ACS chemical biology · 2021Article
- Inhibitory mechanism of reveromycin A at the tRNA binding site of a class I synthetase.Nature communications · 2021Article
- Structural basis of the interaction between cyclodipeptide synthases and aminoacylated tRNA substrates.RNA (New York, N.Y.) · 2020Article
- Two Forms of Tyrosyl-tRNA Synthetase fromSLAS discovery : advancing life sciences R & D · 2020Article
- Correlation between equi-partition of aminoacyl-tRNA synthetases and amino-acid biosynthesis pathways.Nucleic acids research · 2020Article
- Article
36 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial tyrosyl-tRNA synthetases (TyrRS) possess a flexibly linked C-terminal domain of approximately 80 residues, which has hitherto been disordered in crystal structures of the enzyme. We have determined the structure of Thermus thermophilus TyrRS at 2.0 A resolution in a crystal form in which the C-terminal domain is ordered, and confirm that the fold is similar to part of the C-terminal domain of ribosomal protein S4. We have also determined the structure at 2.9 A resolution of the complex of T.thermophilus TyrRS with cognate tRNA(tyr)(G Psi A). In this structure, the C-terminal domain binds between the characteristic long variable arm of the tRNA and the anti-codon stem, thus recognizing the unique shape of the tRNA. The anticodon bases have a novel conformation with A-36 stacked on G-34, and both G-34 and Psi-35 are base-specifically recognized. The tRNA binds across the two subunits of the dimeric enzyme and, remarkably, the mode of recognition of the class I TyrRS for its cognate tRNA resembles that of a class II synthetase in being from the major groove side of the acceptor stem.
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