28sr: Difference between revisions
New page: left|200px<br /><applet load="28sr" size="350" color="white" frame="true" align="right" spinBox="true" caption="28sr" /> '''NMR STRUCTURE OF THE MOST CONSERVED RNA MOTI... |
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== | ==NMR STRUCTURE OF THE MOST CONSERVED RNA MOTIF IN SRP RNA== | ||
The signal recognition particle (SRP) directs translating ribosomes to the | <StructureSection load='28sr' size='340' side='right'caption='[[28sr]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[28sr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=28SR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=28SR 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=28sr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=28sr OCA], [https://pdbe.org/28sr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=28sr RCSB], [https://www.ebi.ac.uk/pdbsum/28sr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=28sr ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The signal recognition particle (SRP) directs translating ribosomes to the protein translocation apparatus of endoplasmic reticulum (ER) membrane or the bacterial plasma membrane. The SRP is universally conserved, and in prokaryotes consists of two essential subunits, SRP RNA and SRP54, the latter of which binds to signal sequences on the nascent protein chains. Here we describe the solution NMR structure of a 28-mer RNA composing the most conserved part of SRP RNA to which SRP54 binds. Central to this function is a six-nucleotide internal loop that assumes a novel Mg2+-dependent structure with unusual cross-strand interactions; besides a cross-strand A/A stack, two guanines form hydrogen bonds with opposite-strand phosphates. The structure completely explains the phylogenetic conservation of the loop bases, underlining its importance for SRP54 binding and SRP function. | |||
Structure of the most conserved internal loop in SRP RNA.,Schmitz U, James TL, Lukavsky P, Walter P Nat Struct Biol. 1999 Jul;6(7):634-8. PMID:10404218<ref>PMID:10404218</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 28sr" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: James | [[Category: James TL]] | ||
[[Category: Lukavsky | [[Category: Lukavsky P]] | ||
[[Category: Schmitz | [[Category: Schmitz U]] | ||
[[Category: Walter | [[Category: Walter P]] | ||
