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Crystal Structure of the Eukaryotic Ribosome

Authors: Gulnara Yusupova; Marat Yusupov; Adam Ben-Shem; Lasse Jenner;

Crystal Structure of the Eukaryotic Ribosome

Abstract

Macromolecular Message Translation The ribosome is a macromolecular machine that translates the sequence of messenger RNA into proteins in all living cells. Structures of prokaryotic ribosomes have supplied insight into the conserved features of such protein synthesis; however, eukaryotic translation has additional levels of complexity. Ben-Shem et al. (p. 1203 ) have determined the crystal structure of the yeast 80S ribosome at 4.15 angstrom resolution. The ribosome is in a ratcheted conformation, which is a state that is an intermediate in the translocation of messenger RNA and transfer RNA. The crystal structure provides the molecular underpinning for existing biochemical and genetic data and will inform the design of functional experiments.

Keywords

Models, Molecular, Ribosomal Proteins, Ribosome Subunits, Small, Eukaryotic, Saccharomyces cerevisiae Proteins, Protein Conformation, RNA, Fungal, Saccharomyces cerevisiae, Ribosome Subunits, Large, Eukaryotic, Crystallography, X-Ray, RNA, Transfer, RNA, Ribosomal, Protein Biosynthesis, Nucleic Acid Conformation, RNA, Messenger, Crystallization, Peptide Chain Initiation, Translational, Ribosomes, Protein Binding

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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
364
Top 1%
Top 1%
Top 0.1%
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