4lvv

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<StructureSection load='4lvv' size='340' side='right'caption='[[4lvv]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='4lvv' size='340' side='right'caption='[[4lvv]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4lvv]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3sd1 3sd1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LVV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LVV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4lvv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_mutans Streptococcus mutans]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3sd1 3sd1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LVV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LVV 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=FFO:N-[4-({[(6S)-2-AMINO-5-FORMYL-4-OXO-3,4,5,6,7,8-HEXAHYDROPTERIDIN-6-YL]METHYL}AMINO)BENZOYL]-L-GLUTAMIC+ACID'>FFO</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sd3|3sd3]], [[4lvw|4lvw]], [[4lvx|4lvx]], [[4lvy|4lvy]], [[4lvz|4lvz]], [[4lw0|4lw0]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FFO:N-[4-({[(6S)-2-AMINO-5-FORMYL-4-OXO-3,4,5,6,7,8-HEXAHYDROPTERIDIN-6-YL]METHYL}AMINO)BENZOYL]-L-GLUTAMIC+ACID'>FFO</scene></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=4lvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lvv OCA], [http://pdbe.org/4lvv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lvv RCSB], [http://www.ebi.ac.uk/pdbsum/4lvv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lvv ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4lvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lvv OCA], [https://pdbe.org/4lvv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lvv RCSB], [https://www.ebi.ac.uk/pdbsum/4lvv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lvv ProSAT]</span></td></tr>
</table>
</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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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 4lvv" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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*[[Riboswitch|Riboswitch]]
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*[[Riboswitch 3D structures|Riboswitch 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Batey, R T]]
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[[Category: Streptococcus mutans]]
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[[Category: Trausch, J J]]
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[[Category: Batey RT]]
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[[Category: Aptamer]]
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[[Category: Trausch JJ]]
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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: Pseudoknot]]
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[[Category: Regulation]]
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[[Category: Rna]]
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[[Category: S-adenosylmethionine]]
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[[Category: Streptococcus mutan]]
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[[Category: Terminator region]]
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[[Category: Tetrahydrofolate]]
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[[Category: Thermodynamic]]
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[[Category: Thf binding]]
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[[Category: Three-way junction]]
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[[Category: Transcription]]
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Current revision

Structure of the THF riboswitch

PDB ID 4lvv

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