ArticleNucleic acids research2011
C-terminal domain of archaeal O-phosphoseryl-tRNA kinase displays large-scale motion to bind the 7-bp D-stem of archaeal tRNA(Sec).
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- PSTK exerts protective role in cisplatin-tubular cell injury via BAX/BCL2/Caspase3 pathway.Physiological reports · 2025Article
- Unconventional genetic code systems in archaea.Frontiers in microbiology · 2022Review
- Trypanosomatid selenophosphate synthetase structure, function and interaction with selenocysteine lyase.PLoS neglected tropical diseases · 2020Article
- Naturally Occurring tRNAs With Non-canonical Structures.Frontiers in microbiology · 2020Review
- Kti12, a PSTK-like tRNA dependent ATPase essential for tRNA modification by Elongator.Nucleic acids research · 2019Article
- Toxin ζ Reduces the ATP and Modulates the Uridine Diphosphate-N-acetylglucosamine Pool.Toxins · 2019Article
- Insights into substrate promiscuity of human seryl-tRNA synthetase.RNA (New York, N.Y.) · 2017Article
- Biophysical analysis ofThe Journal of biological chemistry · 2017Article
- Computational identification of the selenocysteine tRNA (tRNASec) in genomes.PLoS computational biology · 2017Article
- RNA folding pathways in stop motion.Nucleic acids research · 2016Article
- Selenoproteins: molecular pathways and physiological roles.Physiological reviews · 2014Review
- Tertiary structure of bacterial selenocysteine tRNA.Nucleic acids research · 2013Article
- Crystal structure analysis reveals functional flexibility in the selenocysteine-specific tRNA from mouse.PloS one · 2011Article
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Authors and funding
7 authors at 1 institution in 2 countries.
Funding
Abstract
O-Phosphoseryl-tRNA kinase (PSTK) is the key enzyme in recruiting selenocysteine (Sec) to the genetic code of archaea and eukaryotes. The enzyme phosphorylates Ser-tRNA(Sec) to produce O-phosphoseryl-tRNA(Sec) (Sep-tRNA(Sec)) that is then converted to Sec-tRNA(Sec) by Sep-tRNA:Sec-tRNA synthase. Earlier we reported the structure of the Methanocaldococcus jannaschii PSTK (MjPSTK) complexed with AMPPNP. This study presents the crystal structure (at 2.4-Å resolution) of MjPSTK complexed with an anticodon-stem/loop truncated tRNA(Sec) (Mj*tRNA(Sec)), a good enzyme substrate. Mj*tRNA(Sec) is bound between the enzyme's C-terminal domain (CTD) and N-terminal kinase domain (NTD) that are connected by a flexible 11 amino acid linker. Upon Mj*tRNA(Sec) recognition the CTD undergoes a 62-Å movement to allow proper binding of the 7-bp D-stem. This large reorganization of the PSTK quaternary structure likely provides a means by which the unique tRNA(Sec) species can be accurately recognized with high affinity by the translation machinery. However, while the NTD recognizes the tRNA acceptor helix, shortened versions of MjPSTK (representing only 60% of the original size, in which the entire CTD, linker loop and an adjacent NTD helix are missing) are still active in vivo and in vitro, albeit with reduced activity compared to the full-length enzyme.
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