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The solution structure of ribosomal protein L18 from Thermus thermophilus reveals a conserved RNA-binding fold
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- Woestenenk, Esmeralda A. (author)
- KTH,Bioteknologi
- Gongadze, George M. (author)
- Shcherbakov, Dmitry V. (author)
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- Rak, Alexey V. (author)
- Garber, Maria B. (author)
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- (creator_code:org_t)
- 2002
- 2002
- English.
- In: Biochemical Journal. - 0264-6021 .- 1470-8728. ; 363:3, s. 553-561
- Journal article (peer-reviewed)
Abstract
Subject headings
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Keyword
- NMR spectroscopy
- Protein structure
- Ribosome
- RNA-binding protein
- Biology
- Biologi
Publication and Content Type
- ref (subject category)
- art (subject category)
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