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6W2S

Structure of the Cricket Paralysis Virus 5-UTR IRES (CrPV 5-UTR-IRES) bound to the small ribosomal subunit in the open state (Class 1)

This is a non-PDB format compatible entry.
Summary for 6W2S
Entry DOI10.2210/pdb6w2s/pdb
EMDB information21529
Descriptor18S rRNA, uS4, uS17, ... (45 entities in total)
Functional Keywordscrpv 5'-utr ires, internal ribosome entry site, ribosome, ribosome-translation complex, ribosome/translation
Biological sourceCricket paralysis virus
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Total number of polymer chains43
Total formula weight1840048.79
Authors
Neupane, R.,Pisareva, V.,Rodriguez, C.F.,Pisarev, A.,Fernandez, I.S. (deposition date: 2020-03-08, release date: 2020-04-22, Last modification date: 2024-03-06)
Primary citationNeupane, R.,Pisareva, V.P.,Rodriguez, C.F.,Pisarev, A.V.,Fernandez, I.S.
A complex IRES at the 5'-UTR of a viral mRNA assembles a functional 48S complex via an uAUG intermediate.
Elife, 9:-, 2020
Cited by
PubMed Abstract: Taking control of the cellular apparatus for protein production is a requirement for virus progression. To ensure this control, diverse strategies of cellular mimicry and/or ribosome hijacking have evolved. The initiation stage of translation is especially targeted as it involves multiple steps and the engagement of numerous initiation factors. The use of structured RNA sequences, called nternal ibosomal ntry ites (IRES), in viral RNAs is a widespread strategy for the exploitation of eukaryotic initiation. Using a combination of electron cryo-microscopy (cryo-EM) and reconstituted translation initiation assays with native components, we characterized how a novel IRES at the 5'-UTR of a viral RNA assembles a functional initiation complex via an uAUG intermediate. The IRES features a novel extended, multi-domain architecture, that circles the 40S head. The structures and accompanying functional data illustrate the importance of 5'-UTR regions in translation regulation and underline the relevance of the untapped diversity of viral IRESs.
PubMed: 32286223
DOI: 10.7554/eLife.54575
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.47 Å)
Structure validation

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