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  • Woestenenk, Esmeralda A., et al. (author)
  • The solution structure of ribosomal protein L18 from Thermus thermophilus reveals a conserved RNA-binding fold
  • 2002
  • In: Biochemical Journal. - 0264-6021 .- 1470-8728. ; 363:3, s. 553-561
  • Journal article (peer-reviewed)abstract
    • We have determined the solution structure of ribosomal protein L18 from Thermus thermophilus. L18 is a 12.5 kDa protein of the large subunit of the ribosome and binds to both 5 S and 23 S rRNA. In the uncomplexed state L18 folds to a mixed α/β globular structure with a long disordered N-terminal region. We compared our high-resolution structure with RNA-complexed L 18 from Haloarcula marismortui and T. thermophilus to examine RNA-induced as well as species-dependent structural differences. We also identified T. thermophilus S11 as a structural homologue and found that the structures of the RNA-recognition sites are conserved. Important features, for instance a bulge in the RNA-contacting β-sheet, are conserved in both proteins. We suggest that the L18 fold recognizes a specific RNA motif and that the resulting RNA-protein-recognition module is tolerant to variations in sequence.
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  • Result 1-1 of 1
Type of publication
journal article (1)
Type of content
peer-reviewed (1)
Author/Editor
Berglund, Helena (1)
Härd, Torleif (1)
Woestenenk, Esmerald ... (1)
Gongadze, George M. (1)
Shcherbakov, Dmitry ... (1)
Rak, Alexey V. (1)
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Garber, Maria B. (1)
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University
Royal Institute of Technology (1)
Language
English (1)
Research subject (UKÄ/SCB)
Natural sciences (1)
Year
2002 (1)

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