1ILY

Solution Structure of Ribosomal Protein L18 of Thermus thermophilus

Summary for 1ILY

• Entry DOI: 10.2210/pdb1ily/pdb
• NMR Information: BMRB: 4688
• Descriptor: RIBOSOMAL PROTEIN L18 (1 entity in total)
• Functional Keywords: mixed alpha/beta, rna binding protein
• Biological source: Thermus thermophilus
• Total number of polymer chains: 1
• Total formula weight: 9869.51

Authors

Woestenenk, E.A.,Gongadze, G.M.,Shcherbakov, D.V.,Rak, A.V.,Garber, M.B.,Hard, T.,Berglund, H. (deposition date: 2001-05-09, release date: 2002-05-01, Last modification date: 2024-05-22)

Primary citation

Woestenenk, E.A.,Gongadze, G.M.,Shcherbakov, D.V.,Rak, A.V.,Garber, M.B.,Hard, T.,Berglund, H.
The solution structure of ribosomal protein L18 from Thermus thermophilus reveals a conserved RNA-binding fold.
Biochem.J., 363:553-561, 2002

PubMed 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 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.

PubMed: 11964156
DOI: 10.1042/0264-6021:3630553

Experimental method

SOLUTION NMR