22av: Difference between revisions
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==Cryo-EM structure of NSUN2-tRNATyr-SAM== | |||
<StructureSection load='22av' size='340' side='right'caption='[[22av]], [[Resolution|resolution]] 3.34Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[22av]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=22AV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=22AV FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.34Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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=22av FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=22av OCA], [https://pdbe.org/22av PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=22av RCSB], [https://www.ebi.ac.uk/pdbsum/22av PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=22av ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The human RNA m(5)C methyltransferase NSUN2 catalyzes site-specific cytosine methylation across diverse RNA substrates and thereby regulates a wide range of biological and physiological processes. However, the molecular basis by which NSUN2 achieves broad substrate recognition while maintaining catalytic specificity has remained unclear. Here, we determine structures of human NSUN2 in both substrate-free and substrate-bound states using X-ray crystallography and cryo-electron microscopy. Structures of NSUN2 in complex with multiple tRNA substrates reveal a structure-first, sequence-tolerant strategy in which NSUN2 actively remodels tRNA architecture, exposing the buried target cytosine and positioning it within the catalytic pocket for methyl transfer. This recognition strategy enables NSUN2 to accommodate diverse tRNA substrates through a largely conserved interaction interface. Together, our findings define the molecular principles underlying NSUN2-mediated RNA m(5)C modification. | |||
Structure-driven RNA remodeling underlies broad substrate recognition by NSUN2.,Hu Q, Yang W, Yu Y, Yi R, Zhang Y, Duan L, Li F, Zhang K, Gong Q, Li S Sci China Life Sci. 2026 May 26. doi: 10.1007/s11427-026-3373-3. PMID:42258135<ref>PMID:42258135</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 22av" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Hu Q]] | |||
[[Category: Li S]] | |||
[[Category: Yang W]] | |||
[[Category: Zhang K]] | |||
Latest revision as of 04:27, 24 June 2026
Cryo-EM structure of NSUN2-tRNATyr-SAM
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