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TitleStructure of the ribosome-bound cricket paralysis virus IRES RNA.
Journal, issue, pagesNat Struct Mol Biol, Vol. 13, Issue 12, Page 1092-1096, Year 2006
Publish dateNov 19, 2006
AuthorsMartin Schüler / Sean R Connell / Aurelie Lescoute / Jan Giesebrecht / Marylena Dabrowski / Birgit Schroeer / Thorsten Mielke / Pawel A Penczek / Eric Westhof / Christian M T Spahn /
PubMed AbstractInternal ribosome entry sites (IRESs) facilitate an alternative, end-independent pathway of translation initiation. A particular family of dicistroviral IRESs can assemble elongation-competent 80S ...Internal ribosome entry sites (IRESs) facilitate an alternative, end-independent pathway of translation initiation. A particular family of dicistroviral IRESs can assemble elongation-competent 80S ribosomal complexes in the absence of canonical initiation factors and initiator transfer RNA. We present here a cryo-EM reconstruction of a dicistroviral IRES bound to the 80S ribosome. The resolution of the cryo-EM reconstruction, in the subnanometer range, allowed the molecular structure of the complete IRES in its active, ribosome-bound state to be solved. The structure, harboring three pseudoknot-containing domains, each with a specific functional role, shows how defined elements of the IRES emerge from a compactly folded core and interact with the key ribosomal components that form the A, P and E sites, where tRNAs normally bind. Our results exemplify the molecular strategy for recruitment of an IRES and reveal the dynamic features necessary for internal initiation.
External linksNat Struct Mol Biol / PubMed:17115051
MethodsEM (single particle)
Resolution7.3 Å
Structure data

1285

2noq

EMDB-1285: Structure of the ribosome-bound cricket paralysis virus IRES RNA.
PDB-2noq: Structure of ribosome-bound cricket paralysis virus IRES RNA
Method: EM (single particle) / Resolution: 7.3 Å

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsRIBOSOME / IRES RNA / Translation / Internal Initiation

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