Crystal Structure of the Eukaryotic 60S Ribosomal Subunit in Complex with Initiation Factor 6

@article{Klinge2011CrystalSO,
  title={Crystal Structure of the Eukaryotic 60S Ribosomal Subunit in Complex with Initiation Factor 6},
  author={Sebastian Klinge and Felix Voigts-Hoffmann and Marc Leibundgut and Sofia Arpagaus and Nenad Ban},
  journal={Science},
  year={2011},
  volume={334},
  pages={941 - 948}
}
The 3.5 angstrom–resolution structure provides insights into the architecture of the eukaryotic ribosome and its regulation. Protein synthesis in all organisms is catalyzed by ribosomes. In comparison to their prokaryotic counterparts, eukaryotic ribosomes are considerably larger and are subject to more complex regulation. The large ribosomal subunit (60S) catalyzes peptide bond formation and contains the nascent polypeptide exit tunnel. We present the structure of the 60S ribosomal subunit… 

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    Philosophical Transactions of the Royal Society B: Biological Sciences
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...

References

SHOWING 1-10 OF 54 REFERENCES

Crystal Structure of the Eukaryotic 40S Ribosomal Subunit in Complex with Initiation Factor 1

TLDR
The structure provides insight into how protein synthesis is initiated and into the evolution of the eukaryotic ribosome, including the function of eIF1 as well as signaling and regulation mediated by the ribosomal proteins RACK1 and rpS6e.

Crystal Structure of the Eukaryotic Ribosome

TLDR
The crystal structure of the yeast 80S ribosome determined at 4.15 angstrom resolution reveals the higher complexity of eukaryotic ribosomes, which are 40% larger than their bacterial counterparts.

Localization of eukaryote-specific ribosomal proteins in a 5.5-Å cryo-EM map of the 80S eukaryotic ribosome

TLDR
Near-complete atomic models of the 80S ribosome provide insights into the structure, function, and evolution of the eukaryotic translational apparatus.

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

TLDR
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.

Crystal structures of ribosome anti-association factor IF6

TLDR
Comparative protein structure modeling with other known archaeal and eukaryotic homologs demonstrated the presence of two conserved surface regions, one or both of which may bind the large ribosomal subunit.

Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-Å resolution

TLDR
Accurate assignment of the rRNA expansion segments (ES) and variable regions has revealed unique ES–ES and r-protein–ES interactions, providing insight into the structure and evolution of the eukaryotic ribosome.

Powering through ribosome assembly.

TLDR
Ribosome assembly factors such as ATPases, GTPases, and kinases hydrolyze nucleotide triphosphates are reviewed and roles of energy-releasing enzymes in the assembly process are proposed to explain why energy is used for a process that occurs largely spontaneously in bacteria.
...