2ygh
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2ygh is ON HOLD Authors: Schroeder, K., Daldrop, P., Lilley, D. Description: SAM-I riboswitch with a G2nA mutation in the Kink turn in complex with...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==SAM-I riboswitch with a G2nA mutation in the Kink turn in complex with S-adenosylmethionine== | |
| + | <StructureSection load='2ygh' size='340' side='right'caption='[[2ygh]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2ygh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis Caldanaerobacter subterraneus subsp. tengcongensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YGH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YGH FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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=2ygh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ygh OCA], [https://pdbe.org/2ygh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ygh RCSB], [https://www.ebi.ac.uk/pdbsum/2ygh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ygh ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The kink turn is a widespread RNA motif that introduces an acute kink into the axis of duplex RNA, typically comprising a bulge followed by a GA and AG pairs. The kinked conformation is stabilized by metal ions, or the binding of proteins including L7Ae. We now demonstrate a third mechanism for the stabilization of k-turn structure, involving tertiary interactions within a larger RNA structure. The SAM-I riboswitch contains an essential standard k-turn sequence that kinks a helix so that its terminal loop can make a long-range interaction. We find that some sequence variations in the k-turn within the riboswitch do not prevent SAM binding, despite preventing the folding of the k-turn in isolation. Furthermore, two crystal structures show that the sequence-variant k-turns are conventionally folded within the riboswitch. This study shows that the folded structure of the k-turn can be stabilized by tertiary interactions within a larger RNA structure. | ||
| - | + | RNA tertiary interactions in a riboswitch stabilize the structure of a kink turn.,Schroeder KT, Daldrop P, Lilley DM Structure. 2011 Sep 7;19(9):1233-40. PMID:21893284<ref>PMID:21893284</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2ygh" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Riboswitch 3D structures|Riboswitch 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Caldanaerobacter subterraneus subsp. tengcongensis]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Daldrop P]] | ||
| + | [[Category: Lilley D]] | ||
| + | [[Category: Schroeder K]] | ||
Current revision
SAM-I riboswitch with a G2nA mutation in the Kink turn in complex with S-adenosylmethionine
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