9fn2: Difference between revisions

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'''Unreleased structure'''


The entry 9fn2 is ON HOLD  until Paper Publication
==Crystal structure of the alkyltransferase ribozyme SAMURI co-crystallized with SAM==
<StructureSection load='9fn2' size='340' side='right'caption='[[9fn2]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9fn2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9FN2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FN2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1IEA:[(2~{R},3~{S},4~{R},5~{R})-5-(6-azanyl-3-methyl-purin-3-ium-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl+dihydrogen+phosphate'>A1IEA</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=9fn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9fn2 OCA], [https://pdbe.org/9fn2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9fn2 RCSB], [https://www.ebi.ac.uk/pdbsum/9fn2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9fn2 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ribozymes that catalyze site-specific RNA modification have recently gained increasing interest for their ability to mimic methyltransferase enzymes and for their application to install molecular tags. Recently, we reported SAMURI as a site-specific alkyltransferase ribozyme using S-adenosylmethionine (SAM) or a stabilized analog to transfer a methyl or propargyl group to N(3) of an adenosine. Here, we report the crystal structures of SAMURI in the postcatalytic state. The structures reveal a three-helix junction with the catalytic core folded into four stacked layers, harboring the cofactor and the modified nucleotide. Detailed structure-activity analyses explain the cofactor scope and the structural basis for site selectivity. A structural comparison of SAMURI with SAM riboswitches sheds light on how the synthetic ribozyme overcomes the strategies of natural riboswitches to avoid self-methylation. Our results suggest that SAM and its analogs may serve as substrates for various RNA-catalyzed reactions, for which the corresponding ribozymes remain to be identified.


Authors:  
Structure and catalytic activity of the SAM-utilizing ribozyme SAMURI.,Chen HA, Okuda T, Lenz AK, Scheitl CPM, Schindelin H, Hobartner C Nat Chem Biol. 2025 Jan 8. doi: 10.1038/s41589-024-01808-w. PMID:39779902<ref>PMID:39779902</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 9fn2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Chen H-A]]
[[Category: Hoebartner C]]
[[Category: Lenz A-K]]
[[Category: Okuda T]]
[[Category: Scheitl CPM]]
[[Category: Schindelin H]]
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