1ovy: Difference between revisions
No edit summary |
No edit summary |
||
(15 intermediate revisions by the same user not shown) | |||
Line 1: | Line 1: | ||
==Solution Structure of Ribosomal Protein L18 from Bacillus stearothermophilus== | |||
<StructureSection load='1ovy' size='340' side='right'caption='[[1ovy]]' scene=''> | |||
| | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ovy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OVY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OVY 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=1ovy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ovy OCA], [https://pdbe.org/1ovy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ovy RCSB], [https://www.ebi.ac.uk/pdbsum/1ovy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ovy ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RL18_GEOSE RL18_GEOSE] 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. | |||
== 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/ov/1ovy_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=1ovy ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A medium resolution solution structure has been obtained for L18 from Bacillus stearothermophilus (BstL18), a ribosomal protein that stabilizes the tertiary structure of 5S rRNA and mediates its interaction with the rest of the large subunit. The N-terminal 22 amino acid residues of BstL18 are unstructured in solution. Its remaining 98 residues form a globular domain that has the same topology as the globular domains of other L18s, but the orientation of helices is different. This conformational peculiarity should not prevent BstL18 from functioning in the ribosome the same way as other L18s. | |||
The solution structure of ribosomal protein L18 from Bacillus stearothermophilus.,Turner CF, Moore PB J Mol Biol. 2004 Jan 16;335(3):679-84. PMID:14687565<ref>PMID:14687565</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1ovy" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Ribosomal protein L18|Ribosomal protein L18]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
[[Category: Geobacillus stearothermophilus]] | [[Category: Geobacillus stearothermophilus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Moore | [[Category: Moore PB]] | ||
[[Category: Turner | [[Category: Turner CF]] | ||
Latest revision as of 11:57, 22 May 2024
Solution Structure of Ribosomal Protein L18 from Bacillus stearothermophilusSolution Structure of Ribosomal Protein L18 from Bacillus stearothermophilus
Structural highlights
FunctionRL18_GEOSE 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. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA medium resolution solution structure has been obtained for L18 from Bacillus stearothermophilus (BstL18), a ribosomal protein that stabilizes the tertiary structure of 5S rRNA and mediates its interaction with the rest of the large subunit. The N-terminal 22 amino acid residues of BstL18 are unstructured in solution. Its remaining 98 residues form a globular domain that has the same topology as the globular domains of other L18s, but the orientation of helices is different. This conformational peculiarity should not prevent BstL18 from functioning in the ribosome the same way as other L18s. The solution structure of ribosomal protein L18 from Bacillus stearothermophilus.,Turner CF, Moore PB J Mol Biol. 2004 Jan 16;335(3):679-84. PMID:14687565[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
|