The solution structure of ribosomal protein L18 from Thermus thermophilus reveals a conserved RNA-binding fold
| Autor: | Esmeralda A. WOESTENENK, George M. GONGADZE, Dmitry V. SHCHERBAKOV, Alexey V. RAK, Maria B. GARBER, Torleif HÄRD, Helena BERGLUND |
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| Rok vydání: | 2002 |
| Předmět: | |
| Zdroj: | Biochemical Journal. 363:553-561 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj3630553 |
| Popis: | We have determined the solution structure of ribosomal protein L18 from Thermus thermophilus. L18 is a 12.5kDa protein of the large subunit of the ribosome and binds to both 5S and 23S 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 L18 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. |
| Databáze: | OpenAIRE |
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