View source for 9vcu


==Cryo-EM structure of dimeric Suv3-ADP complex==
<StructureSection load='9vcu' size='340' side='right'caption='[[9vcu]], [[Resolution|resolution]] 3.84&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9vcu]] 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=9VCU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9VCU 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]] 3.84&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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=9vcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9vcu OCA], [https://pdbe.org/9vcu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9vcu RCSB], [https://www.ebi.ac.uk/pdbsum/9vcu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9vcu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SUV3_HUMAN SUV3_HUMAN] Major helicase player in mitochondrial RNA metabolism. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. ATPase and ATP-dependent multisubstrate helicase, able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3' direction. Plays a role in the RNA surveillance system in mitochondria; regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates. Also implicated in recombination and chromatin maintenance pathways. May protect cells from apoptosis. Associates with mitochondrial DNA.<ref>PMID:12466530</ref> <ref>PMID:15096047</ref> <ref>PMID:17352692</ref> <ref>PMID:17961633</ref> <ref>PMID:18678873</ref> <ref>PMID:19509288</ref> <ref>PMID:19864255</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human Suv3 is a dimeric helicase that collaborates with the exoribonuclease PNPase to mediate RNA decay and surveillance in mitochondria. Despite its pivotal role in maintaining mitochondrial homeostasis, the molecular mechanism underlying Suv3-mediated RNA unwinding has remained elusive. Here, we present near-atomic-resolution cryogenic electron microscopy structures of Suv3 captured in four functional states: the apo form, two binary complexes with ADP and single-stranded RNA (ssRNA), and a ternary complex with ssRNA and an ATP analog (AMP-PNP). These structures reveal an unexpected asymmetric dimeric organization, in which only one of the two protomers engages in the initial binding of ADP, ssRNA, or both ssRNA and AMP-PNP. Complementary biochemical analyses demonstrate that Suv3 dimerization significantly enhances RNA-binding and unwinding efficiency in an ATP-hydrolysis-dependent manner. Together, these findings provide key insights into the dimeric architecture of Suv3 and establish a mechanistic framework for its coordinated function in processive RNA unwinding.

Asymmetric dimeric assembly of Suv3 helicase facilitates processive RNA unwinding.,Patra M, Jain M, Li YC, Chen YP, Golzarroshan B, Yuan HS Nat Commun. 2026 Apr 15. doi: 10.1038/s41467-026-71901-2. PMID:41986356<ref>PMID:41986356</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9vcu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Patra M]]
[[Category: Yuan HS]]