1ily
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(New page: 200px<br /><applet load="1ily" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ily" /> '''Solution Structure of Ribosomal Protein L18 ...)
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Revision as of 15:22, 20 November 2007
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Solution Structure of Ribosomal Protein L18 of Thermus thermophilus
Overview
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.
About this Structure
1ILY is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
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
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