3B31

Crystal structure of domain III of the Cricket Paralysis Virus IRES RNA

Summary for 3B31

• Entry DOI: 10.2210/pdb3b31/pdb
• Descriptor: RNA (29-MER), RNA (5'-R(P*UP*AP*AP*GP*AP*AP*AP*UP*UP*UP*AP*CP*CP*U)-3'), IRIDIUM HEXAMMINE ION, ... (5 entities in total)
• Functional Keywords: ires, rna structure, translation initiation, trna anticodon, hybrid state, trna mimicry, rna
• Total number of polymer chains: 2
• Total formula weight: 14721.40

Authors

Kieft, J.S.,Costantino, D.A.,Pfingsten, J.S.,Rambo, R.P. (deposition date: 2007-10-19, release date: 2007-12-25, Last modification date: 2024-02-21)

Primary citation

Costantino, D.A.,Pfingsten, J.S.,Rambo, R.P.,Kieft, J.S.
tRNA-mRNA mimicry drives translation initiation from a viral IRES.
Nat.Struct.Mol.Biol., 15:57-64, 2008

PubMed Abstract: Internal ribosome entry site (IRES) RNAs initiate protein synthesis in eukaryotic cells by a noncanonical cap-independent mechanism. IRESes are critical for many pathogenic viruses, but efforts to understand their function are complicated by the diversity of IRES sequences as well as by limited high-resolution structural information. The intergenic region (IGR) IRESes of the Dicistroviridae viruses are powerful model systems to begin to understand IRES function. Here we present the crystal structure of a Dicistroviridae IGR IRES domain that interacts with the ribosome's decoding groove. We find that this RNA domain precisely mimics the transfer RNA anticodon-messenger RNA codon interaction, and its modeled orientation on the ribosome helps explain translocation without peptide bond formation. When combined with a previous structure, this work completes the first high-resolution description of an IRES RNA and provides insight into how RNAs can manipulate complex biological machines.

PubMed: 18157151
DOI: 10.1038/nsmb1351

Experimental method

X-RAY DIFFRACTION (2.4 Å)