The solution structure of ribosomal protein L18 from Thermus thermophilus reveals a conserved RNA-binding fold
2002 (English)In: Biochemical Journal, ISSN 0264-6021, E-ISSN 1470-8728, Vol. 363, no 3, 553-561 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2002. Vol. 363, no 3, 553-561 p.
NMR spectroscopy, Protein structure, Ribosome, RNA-binding protein
IdentifiersURN: urn:nbn:se:kth:diva-5332DOI: 10.1042/0264-6021:3630553ISI: 000175651600015PubMedID: 11964156OAI: oai:DiVA.org:kth-5332DiVA: diva2:8633