Crystal structure of a complex containing domain 3 of crpv igr ires RNA bound to the 70s ribosome. This file contains the 30s subunit of the first 70s ribosome.
Structure:
Ribosomal RNA 16s. Chain: a. 30s ribosomal protein s2. Chain: b. 30s ribosomal protein s3. Chain: c. 30s ribosomal protein s4. Chain: d. 30s ribosomal protein s5.
J.Zhu
et al.
(2011).
Crystal structures of complexes containing domains from two viral internal ribosome entry site (IRES) RNAs bound to the 70S ribosome.
Proc Natl Acad Sci U S A,
108,
1839-1844.
PubMed id: 21245352
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.