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August 20, 2009Science232 citations

Formation of the First Peptide Bond: The Structure of EF-P Bound to the 70 S Ribosome

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GBGregor BlahaUniversity of California, RiversideRSRobin E. StanleyNational Institute of Environmental Health Sciences
Thomas A. Steitz
Thomas A. SteitzNational Institutes of Health

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Abstract

Protein Synthesis Initiation Complex The final step in the initiation phase of protein synthesis is the formation of the first peptide bond, which requires initiator transfer RNA (tRNA) to be bound at the ribosomal P site. Elongation factor P (EF-P) is a protein conserved in all eubacteria that stimulates this initial bond formation. Insight into how this is achieved comes from a structure of Thermus thermophilus 70 S ribosome bound to EF-P, initiator tRNA, and a short piece of messenger RNA presented by Blaha et al. (p. 966 ). EF-P binds between the P and E sites and facilitates proper positioning of initiator tRNA in the P site. A similar mechanism is likely to apply to structurally homologous initiation factors in archea and eukarya.

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Cite This Study

Blaha et al. (2009) studied this question.

synapsesocial.com/papers/69d848077392c8ce61beeb34https://doi.org/10.1126/science.1175800
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Purification and characterization of protein synthesis initiation factors eIF-1, eIF-4C, eIF-4D, and eIF-5 from rabbit reticulocytes.1978 · 154 citations
  2. 2Identification and quantitation of elongation factor EF-P in Escherichia coli cell-free extracts1980 · 27 citations
  3. 3Ribosomal Protein L27 Participates in both 50 S Subunit Assembly and the Peptidyl Transferase Reaction1998 · 77 citations
  4. 4Crystal Structure of the Ribosome at 5.5 Å Resolution2001 · 1,934 citations
  5. 5Identification of a soluble protein that stimulates peptide bond synthesis.1975 · 120 citations