4lvw: Difference between revisions
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==Structure of the THF riboswitch bound to 7-deazaguanine== | |||
<StructureSection load='4lvw' size='340' side='right' caption='[[4lvw]], [[Resolution|resolution]] 1.77Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4lvw]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LVW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LVW FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7DG:7-DEAZAGUANINE'>7DG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sd3|3sd3]], [[4lvv|4lvv]], [[4lvx|4lvx]], [[4lvy|4lvy]], [[4lvz|4lvz]], [[4lw0|4lw0]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lvw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lvw RCSB], [http://www.ebi.ac.uk/pdbsum/4lvw PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The tetrahydrofolate (THF) riboswitch regulates folate transport and metabolism in a number of Firmicutes by cooperatively binding two molecules of THF. To further understand this riboswitch's specificity for THF, binding and regulatory activity of a series of THF analogs and antifolates were examined. Our data reveal that although binding is dominated by the RNA's interactions with the pterin moiety, the para-aminobenzoic acid (pABA) moiety plays a significant role in transcriptional regulation. Further, we find that adenine and several other analogs bind with high affinity by an alternative binding mechanism. Despite a similar affinity to THF, adenine is a poor regulator of transcriptional attenuation. These results demonstrate that binding alone does not determine a compound's effectiveness in regulating the activity of the riboswitch-a complication in current efforts to develop antimicrobials that target these RNAs. | |||
A Disconnect between High-Affinity Binding and Efficient Regulation by Antifolates and Purines in the Tetrahydrofolate Riboswitch.,Trausch JJ, Batey RT Chem Biol. 2014 Feb 20;21(2):205-16. doi: 10.1016/j.chembiol.2013.11.012. Epub, 2014 Jan 2. PMID:24388757<ref>PMID:24388757</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
[[Category: Batey, R T | == References == | ||
[[Category: Trausch, J J | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Batey, R T]] | |||
[[Category: Trausch, J J]] | |||
[[Category: Aptamer]] | [[Category: Aptamer]] | ||
[[Category: Bacillus subtili]] | [[Category: Bacillus subtili]] | ||
