4V7C

Structure of the Ribosome with Elongation Factor G Trapped in the Pre-Translocation State (pre-translocation 70S*tRNA structure)

This is a non-PDB format compatible entry.

Summary for 4V7C

• Entry DOI: 10.2210/pdb4v7c/pdb
• Related: 3J5W 3J5X
• EMDB information: 5799 5800
• Related PRD ID: PRD_000226
• Descriptor: 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (58 entities in total)
• Functional Keywords: translation, ef-g, single particle analysis, pre-translocation translation complex, viomycin
• Biological source: Escherichia coli; More
• Total number of polymer chains: 58
• Total formula weight: 2239893.10

Authors

Brilot, A.F.,Korostelev, A.A.,Ermolenko, D.N.,Grigorieff, N. (deposition date: 2013-11-20, release date: 2014-07-09, Last modification date: 2019-12-18)

Primary citation

Brilot, A.F.,Korostelev, A.A.,Ermolenko, D.N.,Grigorieff, N.
Structure of the ribosome with elongation factor G trapped in the pretranslocation state.
Proc.Natl.Acad.Sci.USA, 110:20994-20999, 2013

PubMed Abstract: During protein synthesis, tRNAs and their associated mRNA codons move sequentially on the ribosome from the A (aminoacyl) site to the P (peptidyl) site to the E (exit) site in a process catalyzed by a universally conserved ribosome-dependent GTPase [elongation factor G (EF-G) in prokaryotes and elongation factor 2 (EF-2) in eukaryotes]. Although the high-resolution structure of EF-G bound to the posttranslocation ribosome has been determined, the pretranslocation conformation of the ribosome bound with EF-G and A-site tRNA has evaded visualization owing to the transient nature of this state. Here we use electron cryomicroscopy to determine the structure of the 70S ribosome with EF-G, which is trapped in the pretranslocation state using antibiotic viomycin. Comparison with the posttranslocation ribosome shows that the small subunit of the pretranslocation ribosome is rotated by ∼12° relative to the large subunit. Domain IV of EF-G is positioned in the cleft between the body and head of the small subunit outwardly of the A site and contacts the A-site tRNA. Our findings suggest a model in which domain IV of EF-G promotes the translocation of tRNA from the A to the P site as the small ribosome subunit spontaneously rotates back from the hybrid, rotated state into the nonrotated posttranslocation state.

PubMed: 24324137
DOI: 10.1073/pnas.1311423110

Experimental method

ELECTRON MICROSCOPY (7.6 Å)