Structural highlights
Function
RL18_THETH This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 alpha/beta 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 beta-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.
The solution structure of ribosomal protein L18 from Thermus thermophilus reveals a conserved RNA-binding fold.,Woestenenk EA, Gongadze GM, Shcherbakov DV, Rak AV, Garber MB, Hard T, Berglund H Biochem J. 2002 May 1;363(Pt 3):553-61. PMID:11964156[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Woestenenk EA, Gongadze GM, Shcherbakov DV, Rak AV, Garber MB, Hard T, Berglund H. The solution structure of ribosomal protein L18 from Thermus thermophilus reveals a conserved RNA-binding fold. Biochem J. 2002 May 1;363(Pt 3):553-61. PMID:11964156
