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

Journal Article · Thu Jan 01 04:00:00 EST 2009 · Science

DOI:https://doi.org/10.1126/science.1175800· OSTI ID:980211

Blaha, G; Stanley, R; Steitz, T

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.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 980211
• Report Number(s): BNL--93129-2010-JA
• Journal Information: Science, Journal Name: Science 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
national synchrotron light source