ArticleNucleic acids research2009
Crystal structure of human selenocysteine tRNA.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 80 citations in OpenAlex.
- Selenoproteins: Minute yet vital players governing cellular fate.Genes & diseases · 2026Review
- Replacing of Cysteine with Selenocysteine: Biochemical Considerations, Computational Modeling, and Protein Engineering Applications.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Crystal structures of free-state tRNARNA (New York, N.Y.) · 2025Article
- Structural Impact of 3-methylcytosine Modification on the Anticodon Stem-loop of a Neuronally-enriched Arginine tRNA.Journal of molecular biology · 2025Article
- Determining the effects of pseudouridine incorporation on human tRNAs.The EMBO journal · 2025Article
- The Unpaved Road of Non-Coding RNA Structure-Function Relationships: Current Knowledge, Available Methodologies, and Future Trends.Non-coding RNA · 2025Review
- Substrate specificity of Mycobacterium tuberculosis tRNA terminal nucleotidyltransferase toxin MenT3.Nucleic acids research · 2024Article
- Bacterial selenocysteine synthase structure revealed by single-particle cryoEM.Current research in structural biology · 2024Article
- A homozygous mutation in the human selenocysteine tRNA gene impairs UGA recoding activity and selenoproteome regulation by selenium.Nucleic acids research · 2023Article
- The Effects of Selenium on Bone Health: From Element to Therapeutics.Molecules (Basel, Switzerland) · 2022Review
- Unconventional genetic code systems in archaea.Frontiers in microbiology · 2022Review
- Pathogenic Variants in Selenoproteins and Selenocysteine Biosynthesis Machinery.International journal of molecular sciences · 2021Review
- Naturally Occurring tRNAs With Non-canonical Structures.Frontiers in microbiology · 2020Review
- Article
- Type-II tRNAs and Evolution of Translation Systems and the Genetic Code.International journal of molecular sciences · 2018Article
- Challenges of site-specific selenocysteine incorporation into proteins by Escherichia coli.RNA biology · 2018Review
- Insights into substrate promiscuity of human seryl-tRNA synthetase.RNA (New York, N.Y.) · 2017Article
- Computational identification of the selenocysteine tRNA (tRNASec) in genomes.PLoS computational biology · 2017Article
- Article
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Selenocysteine (Sec) is the 21st amino acid in translation. Sec tRNA (tRNA(Sec)) has an anticodon complementary to the UGA codon. We solved the crystal structure of human tRNA(Sec). tRNA(Sec) has a 9-bp acceptor stem and a 4-bp T stem, in contrast with the 7-bp acceptor stem and the 5-bp T stem in the canonical tRNAs. The acceptor stem is kinked between the U6:U67 and G7:C66 base pairs, leading to a bent acceptor-T stem helix. tRNA(Sec) has a 6-bp D stem and a 4-nt D loop. The long D stem includes unique A14:U21 and G15:C20a pairs. The D-loop:T-loop interactions include the base pairs G18:U55 and U16:U59, and a unique base triple, U20:G19:C56. The extra arm comprises of a 6-bp stem and a 4-nt loop. Remarkably, the D stem and the extra arm do not form tertiary interactions in tRNA(Sec). Instead, tRNA(Sec) has an open cavity, in place of the tertiary core of a canonical tRNA. The linker residues, A8 and U9, connecting the acceptor and D stems, are not involved in tertiary base pairing. Instead, U9 is stacked on the first base pair of the extra arm. These features might allow tRNA(Sec) to be the target of the Sec synthesis/incorporation machineries.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.