View source for 2khy


==Specifier Domain of B. subtilis tyrS T box leader RNA==
<StructureSection load='2khy' size='340' side='right'caption='[[2khy]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2khy]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KHY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KHY 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=2khy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2khy OCA], [https://pdbe.org/2khy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2khy RCSB], [https://www.ebi.ac.uk/pdbsum/2khy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2khy ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Gram-positive bacteria utilize a tRNA-responsive transcription antitermination mechanism, designated the T box system, to regulate expression of many amino acid biosynthetic and aminoacyl-tRNA synthetase genes. The RNA transcripts of genes controlled by this mechanism contain 5' untranslated regions, or leader RNAs, that specifically bind cognate tRNA molecules through pairing of nucleotides in the tRNA anticodon loop with nucleotides in the Specifier Loop domain of the leader RNA. We have determined the solution structure of the Specifier Loop domain of the tyrS leader RNA from Bacillus subtilis. Fifty percent of the nucleotides in the Specifier Loop domain adopt a loop E motif. The Specifier Sequence nucleotides, which pair with the tRNA anticodon, stack with their Watson-Crick edges rotated toward the minor groove and exhibit only modest flexibility. We also show that a Specifier Loop domain mutation that impairs the function of the B. subtilis glyQS T box RNA disrupts the tyrS loop E motif. Our results suggest a mechanism for tRNA-Specifier Loop binding in which the phosphate backbone kink created by the loop E motif causes the Specifier Sequence bases to rotate toward the minor groove, which increases accessibility for pairing with bases in the anticodon loop of tRNA.

NMR structure and dynamics of the Specifier Loop domain from the Bacillus subtilis tyrS T box leader RNA.,Wang J, Henkin TM, Nikonowicz EP Nucleic Acids Res. 2010 Jun;38(10):3388-98. Epub 2010 Jan 27. PMID:20110252<ref>PMID:20110252</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2khy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Henkin TM]]
[[Category: Wang J]]