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| <StructureSection load='4lw0' size='340' side='right'caption='[[4lw0]], [[Resolution|resolution]] 1.89Å' scene=''> | | <StructureSection load='4lw0' size='340' side='right'caption='[[4lw0]], [[Resolution|resolution]] 1.89Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4lw0]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LW0 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4lw0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_mutans Streptococcus mutans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LW0 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.889Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sd3|3sd3]], [[4lvv|4lvv]], [[4lvw|4lvw]], [[4lvy|4lvy]], [[4lvx|4lvx]], [[4lvz|4lvz]]</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene></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=4lw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lw0 OCA], [http://pdbe.org/4lw0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lw0 RCSB], [http://www.ebi.ac.uk/pdbsum/4lw0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lw0 ProSAT]</span></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=4lw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lw0 OCA], [https://pdbe.org/4lw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lw0 RCSB], [https://www.ebi.ac.uk/pdbsum/4lw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lw0 ProSAT]</span></td></tr> |
| </table> | | </table> |
| <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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| 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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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4lw0" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Riboswitch|Riboswitch]] | | *[[Riboswitch 3D structures|Riboswitch 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Batey, R T]]
| | [[Category: Streptococcus mutans]] |
| [[Category: Trausch, J J]]
| | [[Category: Batey RT]] |
| [[Category: Adenine binding]]
| | [[Category: Trausch JJ]] |
| [[Category: Aptamer]]
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| [[Category: Bacillus subtili]]
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| [[Category: Bacterial]]
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| [[Category: Bacterial protein]]
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| [[Category: Base sequence]]
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| [[Category: Binding site]]
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| [[Category: Calorimetry]]
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| [[Category: Folic acid]]
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| [[Category: Gene expression regulation]]
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| [[Category: Genetic]]
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| [[Category: Guanine]]
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| [[Category: Leucovorin]]
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| [[Category: Ligand]]
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| [[Category: Magnesium]]
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| [[Category: Molecular sequence data]]
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| [[Category: Mrna]]
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| [[Category: Ncrna]]
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| [[Category: Nucleic acid conformation]]
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| [[Category: Nucleotide]]
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| [[Category: Point mutation]]
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| [[Category: Protein binding]]
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| [[Category: Protein structure]]
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| [[Category: Pseudoknot]]
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| [[Category: Regulation]]
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| [[Category: Riboswitch]]
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| [[Category: Rna]]
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| [[Category: S-adenosylmethionine]]
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| [[Category: Secondary]]
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| [[Category: Streptococcus mutan]] | |
| [[Category: Terminator region]] | |
| [[Category: Tetrahydrofolate]] | |
| [[Category: Thermodynamic]]
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| [[Category: Three-way junction]]
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| [[Category: Transcription]]
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