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

Journal Article · Wed Oct 21 04:00:00 EDT 2009 · Science

DOI:https://doi.org/10.1126/science.1175800· OSTI ID:1005864

Blaha, Gregor; Stanley, Robin E; Steitz, Thomas A; Yale,

Elongation factor P (EF-P) is an essential protein that stimulates the formation of the first peptide bond in protein synthesis. Here we report the crystal structure of EF-P bound to the Thermus thermophilus 70S ribosome along with the initiator transfer RNA N-formyl-methionyl-tRNAi (fMet-tRNA{sub i}{sup fMet}) and a short piece of messenger RNA (mRNA) at a resolution of 3.5 angstroms. EF-P binds to a site located between the binding site for the peptidyl tRNA (P site) and the exiting tRNA (E site). It spans both ribosomal subunits with its amino-terminal domain positioned adjacent to the aminoacyl acceptor stem and its carboxyl-terminal domain positioned next to the anticodon stem-loop of the P site-bound initiator tRNA. Domain II of EF-P interacts with the ribosomal protein L1, which results in the largest movement of the L1 stalk that has been observed in the absence of ratcheting of the ribosomal subunits. EF-P facilitates the proper positioning of the fMet-tRNA{sub i}{sup fMet} for the formation of the first peptide bond during translation initiation.

• Research Organization: Argonne National Laboratory (ANL)
• Sponsoring Organization: USDOE
• OSTI ID: 1005864
• Journal Information: Science, Journal Name: Science Journal Issue: 08, 2009 Vol. 325; ISSN 0193-4511; ISSN SCEHDK
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

36 MATERIALS SCIENCE
CRYSTAL STRUCTURE
ELONGATION
MESSENGER-RNA
PEPTIDES
POSITIONING
PROTEINS
RATCHETING
RESOLUTION
RIBOSOMES
SYNTHESIS
TRANSFER RNA