View source for 8sup


==Structure of the 48S translation initiation complex assembled on the encephalomyocarditis virus IRES==
<StructureSection load='8sup' size='340' side='right'caption='[[8sup]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8sup]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Encephalomyocarditis_virus Encephalomyocarditis virus] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8SUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SUP 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]] 3.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=8sup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8sup OCA], [https://pdbe.org/8sup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8sup RCSB], [https://www.ebi.ac.uk/pdbsum/8sup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8sup ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The encephalomyocarditis virus (EMCV) IRES and other Type 2 IRESs comprise domains H-L and specifically interact with eIF4G/eIF4A through their essential JK domain. However, the JK domain is not sufficient for IRES function, which also requires the preceding domain I of unknown function. To identify interactions that drive ribosomal recruitment of eIF4G/eIF4A-bound Type 2 IRESs, we determined the cryo-EM structure of 48S initiation complexes formed on the EMCV IRES. It revealed that the apical domain I cloverleaf contacts ribosomal proteins uS13 and uS19 via its Id subdomain and that the essential GNRA tetraloop in subdomain Ic interacts directly with the TpsiC domain of initiator tRNA. Functional assays supported the exceptional role of these interactions for initiation on this IRES. The strong conservation of primary and secondary structures of the apex of domain I among Type 2 IRESs suggests that the reported interactions are a common essential feature of them all.

The mechanism of ribosomal recruitment during translation initiation on Type 2 IRESs.,Bhattacharjee S, Abaeva IS, Brown ZP, Arhab Y, Fallah H, Hellen CUT, Frank J, Pestova TV bioRxiv [Preprint]. 2025 Jun 11:2025.06.11.659010. doi: , 10.1101/2025.06.11.659010. PMID:40568087<ref>PMID:40568087</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8sup" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Encephalomyocarditis virus]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Abaeva IS]]
[[Category: Arhab Y]]
[[Category: Bhattacharjee S]]
[[Category: Brown ZP]]
[[Category: Fallah H]]
[[Category: Frank J]]
[[Category: Hellen CUT]]
[[Category: Jeevan JC]]
[[Category: Pestova TV]]