6hag: Difference between revisions

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'''Unreleased structure'''


The entry 6hag is ON HOLD  until Paper Publication
==The structure of the SAM/SAH-binding riboswitch.==
<StructureSection load='6hag' size='340' side='right' caption='[[6hag]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6hag]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HAG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HAG FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=6hag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hag OCA], [http://pdbe.org/6hag PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hag RCSB], [http://www.ebi.ac.uk/pdbsum/6hag PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hag ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
S-adenosylmethionine (SAM) is a central metabolite since it is used as a methyl group donor in many different biochemical reactions. Many bacteria control intracellular SAM concentrations using riboswitch-based mechanisms. A number of structurally different riboswitch families specifically bind to SAM and mainly regulate the transcription or the translation of SAM-biosynthetic enzymes. In addition, a highly specific riboswitch class recognizes S-adenosylhomocysteine (SAH)-the product of SAM-dependent methyl group transfer reactions-and regulates enzymes responsible for SAH hydrolysis. High-resolution structures are available for many of these riboswitch classes and illustrate how they discriminate between the two structurally similar ligands SAM and SAH. The so-called SAM/SAH riboswitch class binds both ligands with similar affinities and is structurally not yet characterized. Here, we present a high-resolution nuclear magnetic resonance structure of a member of the SAM/SAH-riboswitch class in complex with SAH. Ligand binding induces pseudoknot formation and sequestration of the ribosome binding site. Thus, the SAM/SAH-riboswitches are translational 'OFF'-switches. Our results establish a structural basis for the unusual bispecificity of this riboswitch class. In conjunction with genomic data our structure suggests that the SAM/SAH-riboswitches might be an evolutionary late invention and not a remnant of a primordial RNA-world as suggested for other riboswitches.


Authors: Weickhmann, A.K.
The structure of the SAM/SAH-binding riboswitch.,Weickhmann AK, Keller H, Wurm JP, Strebitzer E, Juen MA, Kremser J, Weinberg Z, Kreutz C, Duchardt-Ferner E, Wohnert J Nucleic Acids Res. 2018 Dec 27. pii: 5264287. doi: 10.1093/nar/gky1283. PMID:30590743<ref>PMID:30590743</ref>


Description: The structure of the SAM/SAH-binding riboswitch.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Weickhmann, A.K]]
<div class="pdbe-citations 6hag" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Weickhmann, A K]]
[[Category: Pseudoknot]]
[[Category: Riboswitch]]
[[Category: Rna]]
[[Category: Sah]]
[[Category: Sam]]
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