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Science 21 August 2009:
Vol. 325. no. 5943, pp. 966 - 970
DOI: 10.1126/science.1175800
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Research Articles

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

Gregor Blaha,1,* Robin E. Stanley,1,* Thomas A. Steitz1,2,3,{dagger}

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-tRNAifMet) 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-tRNAifMet for the formation of the first peptide bond during translation initiation.

1 Departments of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
2 Department of Chemistry, Yale University, New Haven, CT 06520, USA.
3 Howard Hughes Medical Institute, Yale University, New Haven, CT 06520–8114, USA.

* These authors contributed equally to this work.

{dagger} To whom correspondence should be addressed. E-mail: thomas.steitz{at}yale.edu

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Leaps in Translational Elongation.
A. Liljas (2009)
Science 326, 677-678
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