5btp: Difference between revisions
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==Fusobacterium ulcerans ZTP riboswitch bound to ZMP== | ==Fusobacterium ulcerans ZTP riboswitch bound to ZMP== | ||
<StructureSection load='5btp' size='340' side='right' caption='[[5btp]], [[Resolution|resolution]] 2.82Å' scene=''> | <StructureSection load='5btp' size='340' side='right' caption='[[5btp]], [[Resolution|resolution]] 2.82Å' scene=''> | ||
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<table><tr><td colspan='2'>[[5btp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BTP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BTP FirstGlance]. <br> | <table><tr><td colspan='2'>[[5btp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BTP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BTP FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMZ:AMINOIMIDAZOLE+4-CARBOXAMIDE+RIBONUCLEOTIDE'>AMZ</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMZ:AMINOIMIDAZOLE+4-CARBOXAMIDE+RIBONUCLEOTIDE'>AMZ</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5btp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5btp OCA], [http://pdbe.org/5btp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5btp RCSB], [http://www.ebi.ac.uk/pdbsum/5btp PDBsum]</span></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=5btp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5btp OCA], [http://pdbe.org/5btp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5btp RCSB], [http://www.ebi.ac.uk/pdbsum/5btp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5btp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5btp" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5btp" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Riboswitch|Riboswitch]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 21:05, 16 November 2017
Fusobacterium ulcerans ZTP riboswitch bound to ZMPFusobacterium ulcerans ZTP riboswitch bound to ZMP
Structural highlights
Publication Abstract from PubMedThe bacterial alarmone 5-aminoimidazole-4-carboxamide riboside 5'-triphosphate (AICAR triphosphate or ZTP), derived from the monophosphorylated purine precursor ZMP, accumulates during folate starvation. ZTP regulates genes involved in purine and folate metabolism through a cognate riboswitch. The linker connecting this riboswitch's two subdomains varies in length by over 100 nucleotides. We report the cocrystal structure of the Fusobacterium ulcerans riboswitch bound to ZMP, which spans the two subdomains whose interface also comprises a pseudoknot and ribose zipper. The riboswitch recognizes the carboxamide oxygen of ZMP through an unprecedented inner-sphere coordination with a Mg2+ ion. We show that the affinity of the riboswitch for ZMP is modulated by the linker length. Notably, ZMP can simultaneously bind to the two subdomains even when they are synthesized as separate RNAs. The ZTP riboswitch demonstrates how specific small-molecule binding can drive association of distant noncoding-RNA domains to regulate gene expression. Recognition of the bacterial alarmone ZMP through long-distance association of two RNA subdomains.,Jones CP, Ferre-D'Amare AR Nat Struct Mol Biol. 2015 Aug 17. doi: 10.1038/nsmb.3073. PMID:26280533[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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