ArticleProceedings of the National Academy of Sciences of the United States of America2009
Structure of a tRNA-dependent kinase essential for selenocysteine decoding.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Kti12, a PSTK-like tRNA dependent ATPase essential for tRNA modification by Elongator.Nucleic acids research · 2019Article
- Computational identification of the selenocysteine tRNA (tRNASec) in genomes.PLoS computational biology · 2017Article
- Dimer-dimer interaction of the bacterial selenocysteine synthase SelA promotes functional active-site formation and catalytic specificity.Journal of molecular biology · 2014Article
- Synthesis and decoding of selenocysteine and human health.Croatian medical journal · 2012Review
- Deprotonated imidodiphosphate in AMPPNP-containing protein structures.Acta crystallographica. Section D, Biological crystallography · 2011Article
- C-terminal domain of archaeal O-phosphoseryl-tRNA kinase displays large-scale motion to bind the 7-bp D-stem of archaeal tRNA(Sec).Nucleic acids research · 2011Article
- Crystal structure analysis reveals functional flexibility in the selenocysteine-specific tRNA from mouse.PloS one · 2011Article
- Selenocysteine, pyrrolysine, and the unique energy metabolism of methanogenic archaea.Archaea (Vancouver, B.C.) · 2010Review
- Human SepSecS or SLA/LP: selenocysteine formation and autoimmune hepatitis.Biological chemistry · 2010Review
- Distinct genetic code expansion strategies for selenocysteine and pyrrolysine are reflected in different aminoacyl-tRNA formation systems.FEBS letters · 2010Review
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Compared to bacteria, archaea and eukaryotes employ an additional enzyme for the biosynthesis of selenocysteine (Sec), the 21(st) natural amino acid (aa). An essential RNA-dependent kinase, O-phosphoseryl-tRNA(Sec) kinase (PSTK), converts seryl-tRNA(Sec) to O-phosphoseryl-tRNA(Sec), the immediate precursor of selenocysteinyl-tRNA(Sec). The sequence of Methanocaldococcus jannaschii PSTK (MjPSTK) suggests an N-terminal kinase domain (177 aa) followed by a presumed tRNA binding region (75 aa). The structures of MjPSTK complexed with ADP and AMPPNP revealed that this enzyme belongs to the P-loop kinase class, and that the kinase domain is closely related to gluconate kinase and adenylate kinase. ATP is bound by the P-loop domain (residues 11-18). Formed by antiparallel dimerization of two PSTK monomers, the enzyme structure shows a deep groove with positive electrostatic potential. Located in this groove is the enzyme's active site, which biochemical and genetic data suggest is composed of Asp-41, Arg-44, Glu-55, Tyr-82, Tyr-83, Met-86, and Met-132. Based on structural comparison with Escherichia coli adenylate kinase a docking model was generated that assigns these amino acids to the recognition of the terminal A76-Ser moieties of Ser-tRNA(Sec). The geometry and electrostatic environment of the groove in MjPSTK are perfectly complementary to the unusually long acceptor helix of tRNA(Sec).
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