Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements

@article{Korostelev2014CrystalSO,
  title={Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements},
  author={Andrei A. Korostelev and Sergei Trakhanov and Martin Laurberg and Harry F. Noller},
  journal={Cell},
  year={2014},
  volume={126},
  pages={1065-1077}
}

Figures and Tables from this paper

The ribosome in focus: new structures bring new insights.

Insights into protein biosynthesis from structures of bacterial ribosomes.

  • V. BerkJ. Cate
  • Biology, Chemistry
    Current opinion in structural biology
  • 2007

Structural Studies of the Functional Complexes of the 50S and 70S Ribosome, a Major Antibiotic Target

Our crystal structure of the Haloarcula marismortui (H.ma.) 50S ribosomal subunit and its complexes with substrates and antibiotics have illuminated the mechanism of peptide bond formation and its

Crystal structure of the ribosome recycling factor bound to the ribosome

The crystal structure of the Thermus thermophilus RRF bound to a 70S ribosomal complex containing a stop codon in the A site, a transfer RNA anticodon stem-loop in the P site and tRNAfMet in the E site is described, demonstrating that structures of translation factors bound to 70S Ribosomes can be determined at reasonably high resolution.

Structure of the mammalian 80S ribosome at 8.7 A resolution.

Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome

These structures demonstrate that the PTC is very similar between the 50S subunit and the intact ribosome, and reveal interactions between the ribosomal proteins L16 and L27 and the tRNA substrates, helping to elucidate the role of these proteins in peptidyl transfer.

Structures of the Ribosome in Intermediate States of Ratcheting

Translational Rearrangements Conformational changes in the ribosome are required to translocate messenger RNA and transfer RNA (tRNA) during protein biosynthesis. For example, after peptide bond

Crystal Structures of EF-G–Ribosome Complexes Trapped in Intermediate States of Translocation

The fusidic acid complex (Fus) and two GDPNP complexes (GDPNP-I and GDPNP-II) reveal conformational changes occurring during intermediate states of translocation, including large-scale rotation of the 30S subunit head and 3° to 5° rotation ofthe 30S body during translocation.

Ribosome structure and dynamics during translocation and termination.

The most recent structural models of the bacterial Ribosome that shed light on the movement of messenger RNA and transfer RNA on the ribosome after each peptide bond is formed are described, a process termed translocation.
...

References

SHOWING 1-10 OF 83 REFERENCES

X-ray crystal structures of 70S ribosome functional complexes.

Structures of 70S ribosome complexes containing messenger RNA and transfer RNA (tRNA), or tRNA analogs, have been solved by x-ray crystallography at up to 7.8 angstrom resolution. Many details of the

Crystal Structure of the Ribosome at 5.5 Å Resolution

The crystal structure of the complete Thermus thermophilus 70S ribosome containing bound messenger RNA and transfer RNAs (tRNAs) at 5.5 angstrom resolution is described, suggesting coupling of the 20 to 50 angstrom movements associated with tRNA translocation with intersubunit movement.

Structure of the 30S ribosomal subunit

The crystal structure of the 30S subunit from Thermus thermophilus, refined to 3 Å resolution, is reported, which will facilitate the interpretation in molecular terms of lower resolution structural data on several functional states of the ribosome from electron microscopy and crystallography.

Identification of molecular interactions between P-site tRNA and the ribosome essential for translocation

  • J. FeinbergS. Joseph
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 2001
This work has used a fragmented P-site-bound tRNAMet to identify two 2′-hydroxyl groups at positions 71 and 76 in the 3′-acceptor arm that are essential for translocation.

Structures of the Bacterial Ribosome at 3.5 Å Resolution

Swiveling of the head of the small subunit observed in the present structures, coupled to the ratchet-like motion of the two subunits observed previously, suggests a mechanism for the final movements of messenger RNA and transfer RNAs during translocation.

Ribosomes and translation.

Biochemical and genetic approaches have identified specific functional interactions involving conserved nucleotides in 16S and 23S rRNA and promise to yield an unprecedented view of the mechanism of translation in the coming years.

A ratchet-like inter-subunit reorganization of the ribosome during translocation

Three-dimensional cryo-electron microscopy maps of the Escherichia coli 70S ribosome in various functional states show that both EF-G binding and subsequent GTP hydrolysis lead to ratchet-like rotations of the small 30S sub unit relative to the large 50S subunit, indicating a two-step mechanism of translocation.

The complete atomic structure of the large ribosomal subunit at 2.4 A resolution.

The crystal structure of the large ribosomal subunit from Haloarcula marismortui is determined at 2.4 angstrom resolution, and it includes 2833 of the subunit's 3045 nucleotides and 27 of its 31 proteins.
...