2NOQ

Structure of ribosome-bound cricket paralysis virus IRES RNA

Summary for 2NOQ

• Entry DOI: 10.2210/pdb2noq/pdb
• EMDB information: 1285
• Descriptor: CrPV IRES, 18S ribosomal RNA, 25S ribosomal RNA, ... (8 entities in total)
• Functional Keywords: ires rna, ribosome, translation, internal initiation
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Cytoplasm (By similarity): P26783; Cytoplasm: Q3E757
• Total number of polymer chains: 8
• Total formula weight: 161191.26

Authors

Schuler, M.,Connell, S.R.,Lescoute, A.,Giesebrecht, J.,Dabrowski, M.,Schroeer, B.,Mielke, T.,Penczek, P.A.,Westhof, E.,Spahn, C.M.T. (deposition date: 2006-10-26, release date: 2006-11-21, Last modification date: 2023-12-27)

Primary citation

Schuler, M.,Connell, S.R.,Lescoute, A.,Giesebrecht, J.,Dabrowski, M.,Schroeer, B.,Mielke, T.,Penczek, P.A.,Westhof, E.,Spahn, C.M.
Structure of the ribosome-bound cricket paralysis virus IRES RNA.
Nat.Struct.Mol.Biol., 13:1092-1096, 2006

PubMed Abstract: 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.

PubMed: 17115051
DOI: 10.1038/nsmb1177

Experimental method

ELECTRON MICROSCOPY (7.3 Å)