6cc1: Difference between revisions
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==Crystal structure of ykoY-alx riboswitch chimera bound to cadmium== | ==Crystal structure of ykoY-alx riboswitch chimera bound to cadmium== | ||
<StructureSection load='6cc1' size='340' side='right' caption='[[6cc1]], [[Resolution|resolution]] 2.54Å' scene=''> | <StructureSection load='6cc1' size='340' side='right'caption='[[6cc1]], [[Resolution|resolution]] 2.54Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6cc1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CC1 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[6cc1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CC1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6CC1 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</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" id="ligandDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</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:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6cc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cc1 OCA], [http://pdbe.org/6cc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cc1 RCSB], [http://www.ebi.ac.uk/pdbsum/6cc1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cc1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Bachas, S T]] | [[Category: Bachas, S T]] | ||
[[Category: Amare, A R.Ferre-D]] | [[Category: Amare, A R.Ferre-D]] | ||
Revision as of 11:56, 11 November 2020
Crystal structure of ykoY-alx riboswitch chimera bound to cadmiumCrystal structure of ykoY-alx riboswitch chimera bound to cadmium
Structural highlights
Publication Abstract from PubMedThe large yybP-ykoY family of bacterial riboswitches is broadly distributed phylogenetically. Previously, these gene-regulatory RNAs were proposed to respond to Mn(2+). X-ray crystallography revealed a binuclear cation-binding pocket. This comprises one hexacoordinate site, with six oxygen ligands, which preorganizes the second, with five oxygen and one nitrogen ligands. The relatively soft nitrogen ligand was proposed to confer affinity for Mn(2+), but how this excludes other soft cations remained enigmatic. By subjecting representative yybP-ykoY riboswitches to diverse cations in vitro, we now find that these RNAs exhibit limited transition metal ion selectivity. Among the cations tested, Cd(2+) and Mn(2+) bind most tightly, and comparison of three new Cd(2+)-bound crystal structures suggests that these riboswitches achieve selectivity by enforcing heptacoordination (favored by high-spin Cd(2+) and Mn(2+), but otherwise uncommon) in the softer site. Remarkably, the Cd(2+)- and Mn(2+)-selective bacterial transcription factor MntR also uses heptacoordination within a binuclear site to achieve selectivity. Convergent Use of Heptacoordination for Cation Selectivity by RNA and Protein Metalloregulators.,Bachas ST, Ferre-D'Amare AR Cell Chem Biol. 2018 May 4. pii: S2451-9456(18)30146-6. doi:, 10.1016/j.chembiol.2018.04.016. PMID:29805037[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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