ArticleNucleic acids research2015
Crystal structure of the full-length bacterial selenocysteine-specific elongation factor SelB.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- The mycobacterial selenocysteine machinery: presence and expression.RNA biology · 2026Article
- Replacing of Cysteine with Selenocysteine: Biochemical Considerations, Computational Modeling, and Protein Engineering Applications.Methods in molecular biology (Clifton, N.J.) · 2026Article
- In Silico Identification of Lead Compounds for Pseudomonas Aeruginosa PqsA Enzyme: Computational Study to Block Biofilm Formation.Biomedicines · 2023Article
- Mechanisms Affecting the Biosynthesis and Incorporation Rate of Selenocysteine.Molecules (Basel, Switzerland) · 2021Review
- Bioinformatic Prediction of an tRNAInternational journal of molecular sciences · 2021Article
- Rational Drug Design forFrontiers in molecular biosciences · 2020Article
- On elongation factor eEFSec, its role and mechanism during selenium incorporation into nascent selenoproteins.Biochimica et biophysica acta. General subjects · 2018Review
- Challenges of site-specific selenocysteine incorporation into proteins by Escherichia coli.RNA biology · 2018Review
- Computational identification of the selenocysteine tRNA (tRNASec) in genomes.PLoS computational biology · 2017Article
- Article
- Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation.Nature communications · 2016Article
- Pre-40S ribosome biogenesis factor Tsr1 is an inactive structural mimic of translational GTPases.Nature communications · 2016Article
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Selenocysteine (Sec), the 21(st) amino acid in translation, uses its specific tRNA (tRNA(Sec)) to recognize the UGA codon. The Sec-specific elongation factor SelB brings the selenocysteinyl-tRNA(Sec) (Sec-tRNA(Sec)) to the ribosome, dependent on both an in-frame UGA and a Sec-insertion sequence (SECIS) in the mRNA. The bacterial SelB binds mRNA through its C-terminal region, for which crystal structures have been reported. In this study, we determined the crystal structure of the full-length SelB from the bacterium Aquifex aeolicus, in complex with a GTP analog, at 3.2-Å resolution. SelB consists of three EF-Tu-like domains (D1-3), followed by four winged-helix domains (WHD1-4). The spacer region, connecting the N- and C-terminal halves, fixes the position of WHD1 relative to D3. The binding site for the Sec moiety of Sec-tRNA(Sec) is located on the interface between D1 and D2, where a cysteine molecule from the crystallization solution is coordinated by Arg residues, which may mimic Sec binding. The Sec-binding site is smaller and more exposed than the corresponding site of EF-Tu. Complex models of Sec-tRNA(Sec), SECIS RNA, and the 70S ribosome suggest that the unique secondary structure of tRNA(Sec) allows SelB to specifically recognize tRNA(Sec) and characteristically place it at the ribosomal A-site.
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