3d2g: Difference between revisions
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==Structural basis of thiamine pyrophosphate analogues binding to the eukaryotic riboswitch== | ==Structural basis of thiamine pyrophosphate analogues binding to the eukaryotic riboswitch== | ||
<StructureSection load='3d2g' size='340' side='right' caption='[[3d2g]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='3d2g' size='340' side='right'caption='[[3d2g]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3d2g]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3d2g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D2G FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3d2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d2g OCA], [https://pdbe.org/3d2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d2g RCSB], [https://www.ebi.ac.uk/pdbsum/3d2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d2g ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3d2g" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Riboswitch|Riboswitch]] | *[[Riboswitch 3D structures|Riboswitch 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thore S]] | ||
Latest revision as of 15:38, 30 August 2023
Structural basis of thiamine pyrophosphate analogues binding to the eukaryotic riboswitchStructural basis of thiamine pyrophosphate analogues binding to the eukaryotic riboswitch
Structural highlights
Publication Abstract from PubMedThe thiamine pyrophosphate (TPP)-sensing riboswitch is the only riboswitch found in eukaryotes. In plants, TPP regulates its own production by binding to the 3' untranslated region of the mRNA encoding ThiC, a critical enzyme in thiamine biosynthesis, which promotes the formation of an unstable splicing variant. In order to better understand the molecular basis of TPP-analogue binding to the eukaryotic TPP-responsive riboswitch, we have determined the crystal structures of the Arabidopsis thaliana TPP-riboswitch in complex with oxythiamine pyrophosphate (OTPP) and with the antimicrobial compound pyrithiamine pyrophosphate (PTPP). The OTPP-riboswitch complex reveals that the pyrimidine ring of OTPP is stabilized in its enol form in order to retain key interactions with guanosine 28 of the riboswitch previously observed in the TPP complex. The structure of PTPP in complex with the riboswitch shows that the base moiety of guanosine 60 undergoes a conformational change to cradle the pyridine ring of the PTPP. Structural information from these complexes has implications for the design of novel antimicrobials targeting TPP-sensing riboswitches. Structural basis of thiamine pyrophosphate analogues binding to the eukaryotic riboswitch.,Thore S, Frick C, Ban N J Am Chem Soc. 2008 Jul 2;130(26):8116-7. Epub 2008 Jun 6. PMID:18533652[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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