3d0x: Difference between revisions
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==Crystal Structure of the unbound lysine riboswitch== | ==Crystal Structure of the unbound lysine riboswitch== | ||
<StructureSection load='3d0x' size='340' side='right' caption='[[3d0x]], [[Resolution|resolution]] 2.95Å' scene=''> | <StructureSection load='3d0x' size='340' side='right'caption='[[3d0x]], [[Resolution|resolution]] 2.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3d0x]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D0X OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[3d0x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D0X FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3d0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d0x OCA], [https://pdbe.org/3d0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d0x RCSB], [https://www.ebi.ac.uk/pdbsum/3d0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d0x 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 3d0x" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Riboswitch 3D structures|Riboswitch 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermotoga maritima]] | ||
[[Category: | [[Category: Batey RT]] | ||
[[Category: | [[Category: Garst AD]] | ||
[[Category: | [[Category: Heroux A]] | ||
[[Category: | [[Category: Rambo RP]] | ||
Latest revision as of 15:36, 30 August 2023
Crystal Structure of the unbound lysine riboswitchCrystal Structure of the unbound lysine riboswitch
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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