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[[Image:1ily.gif|left|200px]]
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{{STRUCTURE_1ily|  PDB=1ily  |  SCENE=  }}
'''Solution Structure of Ribosomal Protein L18 of Thermus thermophilus'''


==Solution Structure of Ribosomal Protein L18 of Thermus thermophilus==
<StructureSection load='1ily' size='340' side='right'caption='[[1ily]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ily]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ILY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ILY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ily FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ily OCA], [https://pdbe.org/1ily PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ily RCSB], [https://www.ebi.ac.uk/pdbsum/1ily PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ily ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RL18_THETH 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/il/1ily_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ily ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==Overview==
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<ref>PMID:11964156</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 1ily" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Ribosomal protein L18|Ribosomal protein L18]]
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Berglund, H.]]
[[Category: Berglund H]]
[[Category: Garber, M B.]]
[[Category: Garber MB]]
[[Category: Gongadze, G M.]]
[[Category: Gongadze GM]]
[[Category: Hard, T.]]
[[Category: Hard T]]
[[Category: Rak, A V.]]
[[Category: Rak AV]]
[[Category: Shcherbakov, D V.]]
[[Category: Shcherbakov DV]]
[[Category: Woestenenk, E A.]]
[[Category: Woestenenk EA]]
[[Category: Mixed alpha/beta]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:08:22 2008''

Latest revision as of 08:35, 22 May 2024

Solution Structure of Ribosomal Protein L18 of Thermus thermophilus

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