3d0u: Difference between revisions
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==Crystal Structure of Lysine Riboswitch Bound to Lysine== | ==Crystal Structure of Lysine Riboswitch Bound to Lysine== | ||
<StructureSection load='3d0u' size='340' side='right' caption='[[3d0u]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='3d0u' size='340' side='right' caption='[[3d0u]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
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<table><tr><td colspan='2'>[[3d0u]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3D0U FirstGlance]. <br> | <table><tr><td colspan='2'>[[3d0u]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3D0U FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IRI:IRIDIUM+HEXAMMINE+ION'>IRI</scene>, <scene name='pdbligand=LYS:LYSINE'>LYS</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IRI:IRIDIUM+HEXAMMINE+ION'>IRI</scene>, <scene name='pdbligand=LYS:LYSINE'>LYS</scene></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=3d0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d0u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3d0u RCSB], [http://www.ebi.ac.uk/pdbsum/3d0u PDBsum]</span></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=3d0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d0u OCA], [http://pdbe.org/3d0u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3d0u RCSB], [http://www.ebi.ac.uk/pdbsum/3d0u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3d0u ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3d0u" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 22:15, 5 August 2016
Crystal Structure of Lysine Riboswitch Bound to LysineCrystal Structure of Lysine Riboswitch Bound to Lysine
Structural highlights
Publication Abstract from PubMedRiboswitches are metabolite-sensitive elements found in mRNAs that control gene expression through a regulatory secondary structural switch. Along with regulation of lysine biosynthetic genes, mutations within the lysine-responsive riboswitch (L-box) play a role in the acquisition of resistance to antimicrobial lysine analogs. To understand the structural basis for lysine binding, we have determined the 2.8 angstroms resolution crystal structure of lysine bound to the Thermotoga maritima asd lysine riboswitch ligand-binding domain. The structure reveals a complex architecture scaffolding a binding pocket completely enveloping lysine. Mutations conferring antimicrobial resistance cluster around this site as well as highly conserved long range interactions, indicating that they disrupt lysine binding or proper folding of the RNA. Comparison of the free and bound forms by x-ray crystallography, small angle x-ray scattering, and chemical probing reveals almost identical structures, indicating that lysine induces only limited and local conformational changes upon binding. Crystal structure of the lysine riboswitch regulatory mRNA element.,Garst AD, Heroux A, Rambo RP, Batey RT J Biol Chem. 2008 Aug 15;283(33):22347-51. Epub 2008 Jul 1. PMID:18593706[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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