1ily: Difference between revisions
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'''Solution Structure of Ribosomal Protein L18 of Thermus thermophilus''' | {{Structure | ||
|PDB= 1ily |SIZE=350|CAPTION= <scene name='initialview01'>1ily</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= RL18 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus]) | |||
}} | |||
'''Solution Structure of Ribosomal Protein L18 of Thermus thermophilus''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ILY is a [ | 1ILY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ILY OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11964156 11964156] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
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[[Category: mixed alpha/beta]] | [[Category: mixed alpha/beta]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:52:02 2008'' | ||
Revision as of 09:52, 20 March 2008
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| Gene: | RL18 (Thermus thermophilus) | ||||||||||||
| 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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