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1ily

From Proteopedia

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|ACTIVITY=
|ACTIVITY=
|GENE= RL18 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])
|GENE= RL18 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ily FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ily OCA], [http://www.ebi.ac.uk/pdbsum/1ily PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ily RCSB]</span>
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[[Category: mixed alpha/beta]]
[[Category: mixed alpha/beta]]
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Revision as of 18:21, 30 March 2008


PDB ID 1ily

Drag the structure with the mouse to rotate
Gene: RL18 (Thermus thermophilus)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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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