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

  title={Crystal Structure of the Eukaryotic 40S Ribosomal Subunit in Complex with Initiation Factor 1},
  author={Julius Rabl and Marc Leibundgut and Sandro F. Ataide and Andrea Haag and Nenad Ban},
  pages={730 - 736}
The structure provides insight into how protein synthesis is initiated and into the evolution of the eukaryotic ribosome. Eukaryotic ribosomes are substantially larger and more complex than their bacterial counterparts. Although their core function is conserved, bacterial and eukaryotic protein synthesis differ considerably at the level of initiation. The eukaryotic small ribosomal subunit (40S) plays a central role in this process; it binds initiation factors that facilitate scanning of… 

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

The 3.5 angstrom–resolution structure of the 60S ribosomal subunit from Tetrahymena thermophila in complex with eukaryotic initiation factor 6 (eIF6), cocrystallized with the antibiotic cycloheximide, elucidates the molecular basis of the interaction with eIF6 and provides a structural framework for further studies of ribosome-associated diseases.

Molecular Architecture of a Eukaryotic Translational Initiation Complex

The use of recent advances in cryo-EM to determine a relatively high-resolution structure of the eIF5B-ribosome complex from a very small fraction of a sample could be a general approach for the study of other dynamic or transient biological complexes.

5.5 Å Structure of the Eukaryotic Ribosome

Cryo-electron microscopy and single-particle reconstruction provide insights into the structure, function and evolution of the eukaryotic translational apparatus with near-complete atomic models of the 80S ribosome.

Crystal structure of eukaryotic ribosome and its complexes with inhibitors

  • G. YusupovaM. Yusupov
  • Biology, Chemistry
    Philosophical Transactions of the Royal Society B: Biological Sciences
  • 2017
The crystal structure of the entire 80S ribosome from yeast is discussed, which reveals its eukaryotic-specific features, and application of X-ray crystallography of the 80S Ribosome for investigation of the binding mode for distinct compounds known to inhibit or modulate the protein-translation function of the ribosomes is referred to.

The Eukaryotic Ribosome

This structure, together with a crystal structure of the eukaryotic ribosome from the yeast Saccharomyces cerevisiae at a resolution of 4.15 Å and a cryoelectron microscopy (cryo-EM) structure of a translating plant ribosomal subunit from Triticum aestivum, represents a breakthrough in studying translation in eUKaryotes.

Eukaryotic Ribosome Biogenesis: The 40S Subunit

The mechanisms underlying these differences are still not well understood, because, unlike yeast, there are no effective methods for characterizing pre-ribosomal complexes in humans.

Extensions, Extra Factors, and Extreme Complexity: Ribosomal Structures Provide Insights into Eukaryotic Translation.

This review highlights the past decade's structural work on eukaryotic ribosomes and its implications on the understanding of eUKaryotic translation.

Assembly of the small ribosomal subunit in yeast: mechanism and regulation.

This review aims to integrate new results from cryo-electron microscopy, X-ray crystallography, and other biochemical and molecular biology methods into an updated view of small sub unit biogenesis and its regulation, in yeast, from transcription to the formation of the mature small subunit.

mRNAs that specifically interact with eukaryotic ribosomal subunits.




Crystal Structure of the Eukaryotic Ribosome

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.

Crystal structure of an initiation factor bound to the 30S ribosomal subunit.

The crystal structure of a complex of IF1 and the 30S ribosomal subunit is reported, explaining how localized changes at the ribosome A site lead to global alterations in the conformation of the30S subunit.

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

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

Initiation of Protein Synthesis in Bacteria

A detailed description of current knowledge about the structure, function, and interactions of the individual components involved in bacterial translation initiation is presented and the mechanisms of regulation of the translation initiation event are provided.

Structure of Monomeric Yeast and Mammalian Sec61 Complexes Interacting with the Translating Ribosome

Subnanometer-resolution cryo–electron microscopy structures of eukaryotic ribosome-Sec61 complexes are determined and it is found that in both idle and active states, the Sec complex is not oligomeric and interacts mainly via two cytoplasmic loops with the universal ribosomal adaptor site.

Structure of a bacterial 30S ribosomal subunit at 5.5 Å resolution

A crystallographic analysis of the structure of the 30S ribosomal subunit from the bacterium Thermus thermophilus shows double-helical regions of RNA to be identified throughout the subunit, and all seven of the small-subunit proteins of known crystal structure to be positioned in the electron density map.