4v6a › Citations

Formation of the first peptide bond: the structure of EF-P bound to the 70S ribosome.

Blaha G, Stanley RE, Steitz TA
Science 325 966-70 (2009)
Cited: 138 times
EuropePMC logo PMID: 19696344

Abstract

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-tRNA(i) (fMet-tRNA(i)(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(i)(fMet) for the formation of the first peptide bond during translation initiation.

Articles - 4v6a mentioned but not cited (3)

  1. Essential structural elements in tRNA(Pro) for EF-P-mediated alleviation of translation stalling. Katoh T, Wohlgemuth I, Nagano M, Rodnina MV, Suga H. Nat Commun 7 11657 (2016)
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  3. Pseudouridine modifications influence binding of aminoglycosides to helix 69 of bacterial ribosomes. Sakakibara Y, Chow CS. Org Biomol Chem 15 8535-8543 (2017)


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