4V6A

Structure of EF-P bound to the 70S ribosome.

This is a non-PDB format compatible entry.

Summary for 4V6A

• Entry DOI: 10.2210/pdb4v6a/pdb
• Descriptor: 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (58 entities in total)
• Functional Keywords: translation, elongation factor, initiation, l1-stalk, ribosome
• Biological source: Thermus thermophilus HB8; More
• Cellular location: Cytoplasm : Q76G20
• Total number of polymer chains: 112
• Total formula weight: 4498367.14

Authors

Stanley, R.E.,Blaha, G. (deposition date: 2009-06-15, release date: 2014-07-09, Last modification date: 2024-11-06)

Primary citation

Blaha, G.,Stanley, R.E.,Steitz, T.A.
Formation of the first peptide bond: the structure of EF-P bound to the 70S ribosome.
Science, 325:966-970, 2009

PubMed 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.

PubMed: 19696344
DOI: 10.1126/science.1175800

Experimental method

X-RAY DIFFRACTION (3.1 Å)