8sup | pdb_00008sup

Structure of the 48S translation initiation complex assembled on the encephalomyocarditis virus IRES

spinqualitylabelsall models 8sup, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8sup is a 10 chain structure with sequence from Encephalomyocarditis virus and Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.1Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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