3ges: Difference between revisions
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<StructureSection load='3ges' size='340' side='right'caption='[[3ges]], [[Resolution|resolution]] 2.15Å' scene=''> | <StructureSection load='3ges' size='340' side='right'caption='[[3ges]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ges]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GES OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[3ges]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GES FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6GO:6-O-METHYLGUANINE'>6GO</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NCO:COBALT+HEXAMMINE(III)'>NCO</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6GO:6-O-METHYLGUANINE'>6GO</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NCO:COBALT+HEXAMMINE(III)'>NCO</scene></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=3ges FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ges OCA], [https://pdbe.org/3ges PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ges RCSB], [https://www.ebi.ac.uk/pdbsum/3ges PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ges 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: Bacillus subtilis]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Batey | [[Category: Batey RT]] | ||
[[Category: Gilbert | [[Category: Gilbert SD]] | ||
Latest revision as of 10:04, 6 September 2023
Crystal structure of the guanine riboswitch C74U mutant bound to 6-O-methylguanineCrystal structure of the guanine riboswitch C74U mutant bound to 6-O-methylguanine
Structural highlights
Publication Abstract from PubMedPurine riboswitches discriminate between guanine and adenine by at least 10,000-fold based on the identity of a single pyrimidine (Y74) that forms a Watson-Crick base pair with the ligand. To understand how this high degree of specificity for closely related compounds is achieved through simple pairing, we investigated their interaction with purine analogs with varying functional groups at the 2- and 6-positions that have the potential to alter interactions with Y74. Using a combination of crystallographic and calorimetric approaches, we find that binding these purines is often facilitated by either small structural changes in the RNA or tautomeric changes in the ligand. This work also reveals that, along with base pairing, conformational restriction of Y74 significantly contributes to nucleobase selectivity. These results reveal that compounds that exploit the inherent local flexibility within riboswitch binding pockets can alter their ligand specificity. Adaptive ligand binding by the purine riboswitch in the recognition of guanine and adenine analogs.,Gilbert SD, Reyes FE, Edwards AL, Batey RT Structure. 2009 Jun 10;17(6):857-68. PMID:19523903[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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