4V84

Crystal structure of a complex containing domain 3 of CrPV IGR IRES RNA bound to the 70S ribosome.

This is a non-PDB format compatible entry.

Summary for 4V84

• Entry DOI: 10.2210/pdb4v84/pdb
• Related: 3PYN 3PYO 3PYQ 3PYR 3PYT 3PYU 3PYV
• Descriptor: ribosomal RNA 16S, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (55 entities in total)
• Functional Keywords: 70s, ribosome, igr, ires, psiv, crpv
• Biological source: Thermus thermophilus HB27; More
• Total number of polymer chains: 106
• Total formula weight: 4282688.60

Authors

Zhu, J.,Korostelev, A.,Costantino, D.,Noller, H.F.,Kieft, J.S. (deposition date: 2010-12-13, release date: 2014-07-09, Last modification date: 2024-10-30)

Primary citation

Zhu, J.,Korostelev, A.,Costantino, D.A.,Donohue, J.P.,Noller, H.F.,Kieft, J.S.
Crystal structures of complexes containing domains from two viral internal ribosome entry site (IRES) RNAs bound to the 70S ribosome.
Proc.Natl.Acad.Sci.USA, 108:1839-1844, 2011

PubMed Abstract: Internal ribosome entry site (IRES) RNAs are elements of viral or cellular mRNAs that bypass steps of canonical eukaryotic cap-dependent translation initiation. Understanding of the structural basis of IRES mechanisms is limited, partially due to a lack of high-resolution structures of IRES RNAs bound to their cellular targets. Prompted by the universal phylogenetic conservation of the ribosomal P site, we solved the crystal structures of proposed P site binding domains from two intergenic region IRES RNAs bound to bacterial 70S ribosomes. The structures show that these IRES domains nearly perfectly mimic a tRNA • mRNA interaction. However, there are clear differences in the global shape and position of this IRES domain in the intersubunit space compared to those of tRNA, supporting a mechanism for IRES action that invokes hybrid state mimicry to drive a noncanonical mode of translocation. These structures suggest how relatively small structured RNAs can manipulate complex biological machines.

PubMed: 21245352
DOI: 10.1073/pnas.1018582108

Experimental method

X-RAY DIFFRACTION (3.4 Å)