3gx2: Difference between revisions
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==TteSAM-I riboswitch variant A94GU34C bound to sinefungin== | ==TteSAM-I riboswitch variant A94GU34C bound to sinefungin== | ||
<StructureSection load='3gx2' size='340' side='right' caption='[[3gx2]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='3gx2' size='340' side='right'caption='[[3gx2]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3gx2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GX2 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[3gx2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GX2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3GX2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SFG:SINEFUNGIN'>SFG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SFG:SINEFUNGIN'>SFG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gx3|3gx3]], [[3gx5|3gx5]], [[3gx6|3gx6]], [[3gx7|3gx7]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gx3|3gx3]], [[3gx5|3gx5]], [[3gx6|3gx6]], [[3gx7|3gx7]]</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=3gx2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gx2 OCA], [http://pdbe.org/3gx2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gx2 RCSB], [http://www.ebi.ac.uk/pdbsum/3gx2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3gx2 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: Batey, R T]] | [[Category: Batey, R T]] | ||
[[Category: Montange, R K]] | [[Category: Montange, R K]] | ||
Revision as of 13:41, 9 September 2020
TteSAM-I riboswitch variant A94GU34C bound to sinefunginTteSAM-I riboswitch variant A94GU34C bound to sinefungin
Structural highlights
Publication Abstract from PubMedThe SAM-I riboswitch is a cis-acting element of genetic control found in bacterial mRNAs that specifically binds S-adenosylmethionine (SAM). We previously determined the 2.9-A X-ray crystal structure of the effector-binding domain of this RNA element, revealing details of RNA-ligand recognition. To improve this structure, variations were made to the RNA sequence to alter lattice contacts, resulting in a 0.5-A improvement in crystallographic resolution and allowing for a more accurate refinement of the crystallographic model. The basis for SAM specificity was addressed by a structural analysis of the RNA complexed to S-adenosylhomocysteine (SAH) and sinefungin and by measuring the affinity of SAM and SAH for a series of mutants using isothermal titration calorimetry. These data illustrate the importance of two universally conserved base pairs in the RNA that form electrostatic interactions with the positively charged sulfonium group of SAM, thereby providing a basis for discrimination between SAM and SAH. Discrimination between closely related cellular metabolites by the SAM-I riboswitch.,Montange RK, Mondragon E, van Tyne D, Garst AD, Ceres P, Batey RT J Mol Biol. 2010 Feb 26;396(3):761-72. Epub 2009 Dec 16. PMID:20006621[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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