4y1m: Difference between revisions
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''' | ==An Escherichia coli yybP-ykoY Mn riboswitch in the Mn2+-free state== | ||
<StructureSection load='4y1m' size='340' side='right' caption='[[4y1m]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== 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 [http://oca.weizmann.ac.il/oca-docs/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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y1i|4y1i]], [[4y1j|4y1j]]</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=4y1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y1m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4y1m RCSB], [http://www.ebi.ac.uk/pdbsum/4y1m PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Gene 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<ref>PMID:25794619</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ke, A]] | [[Category: Ke, A]] | ||
[[Category: Price, I | [[Category: Price, I R]] | ||
[[Category: Free state]] | |||
[[Category: Manganese]] | |||
[[Category: Riboswitch]] | |||
[[Category: Rna]] | |||
Revision as of 14:02, 8 April 2015
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. References
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