4y1m: Difference between revisions
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<StructureSection load='4y1m' size='340' side='right'caption='[[4y1m]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='4y1m' size='340' side='right'caption='[[4y1m]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4y1m]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y1M OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4y1m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y1M FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene></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=4y1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y1m OCA], [https://pdbe.org/4y1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y1m RCSB], [https://www.ebi.ac.uk/pdbsum/4y1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y1m ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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==See Also== | ==See Also== | ||
*[[Riboswitch|Riboswitch]] | *[[Riboswitch 3D structures|Riboswitch 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ke | [[Category: Ke A]] | ||
[[Category: Price | [[Category: Price IR]] | ||
Revision as of 21:03, 26 April 2023
An Escherichia coli yybP-ykoY Mn riboswitch in the Mn2+-free stateAn Escherichia coli yybP-ykoY Mn riboswitch in the Mn2+-free state
Structural highlights
Publication Abstract from PubMedGene regulation in cis by riboswitches is prevalent in bacteria. The yybP-ykoY riboswitch family is quite widespread, yet its ligand and function remained unknown. Here, we characterize the Lactococcus lactis yybP-ykoY orphan riboswitch as a Mn(2+)-dependent transcription-ON riboswitch, with a approximately 30-40 muM affinity for Mn(2+). We further determined its crystal structure at 2.7 A to elucidate the metal sensing mechanism. The riboswitch resembles a hairpin, with two coaxially stacked helices tethered by a four-way junction and a tertiary docking interface. The Mn(2+)-sensing region, strategically located at the highly conserved docking interface, has two metal binding sites. Whereas one site tolerates the binding of either Mg(2+) or Mn(2+), the other site strongly prefers Mn(2+) due to a direct contact from the N7 of an invariable adenosine. Mutagenesis and a Mn(2+)-free E. coli yybP-ykoY structure further reveal that Mn(2+) binding is coupled with stabilization of the Mn(2+)-sensing region and the aptamer domain. Mn(2+)-Sensing Mechanisms of yybP-ykoY Orphan Riboswitches.,Price IR, Gaballa A, Ding F, Helmann JD, Ke A Mol Cell. 2015 Mar 19;57(6):1110-23. doi: 10.1016/j.molcel.2015.02.016. PMID:25794619[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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