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4lvx

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{{STRUCTURE_4lvx| PDB=4lvx | SCENE= }}
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==Structure of the THF riboswitch bound to tetrahydrobiopterin==
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===Structure of the THF riboswitch bound to tetrahydrobiopterin===
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<StructureSection load='4lvx' size='340' side='right' caption='[[4lvx]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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{{ABSTRACT_PUBMED_24388757}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4lvx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LVX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LVX FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sd3|3sd3]], [[4lvv|4lvv]], [[4lvw|4lvw]], [[4lvy|4lvy]], [[4lvz|4lvz]], [[4lw0|4lw0]]</td></tr>
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<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=4lvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lvx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lvx RCSB], [http://www.ebi.ac.uk/pdbsum/4lvx PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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[[4lvx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LVX OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:024388757</ref><references group="xtra"/><references/>
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</div>
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[[Category: Batey, R T.]]
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== References ==
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[[Category: Trausch, J J.]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Batey, R T]]
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[[Category: Trausch, J J]]
[[Category: Aptamer]]
[[Category: Aptamer]]
[[Category: Bacillus subtili]]
[[Category: Bacillus subtili]]

Revision as of 11:18, 25 January 2015

Structure of the THF riboswitch bound to tetrahydrobiopterin

4lvx, resolution 1.90Å

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