Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome

Matthieu Gagnon, Jinzhong Lin, David Bulkley, Thomas A. Steitz

Research output: Contribution to journalArticle

31 Scopus citations

Abstract

Elongation factor 4 (EF4/LepA) is a highly conserved guanosine triphosphatase translation factor. It was shown to promote back-translocation of tRNAs on posttranslocational ribosome complexes and to compete with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis. Here, we report a crystal structure of EF4-guanosine diphosphate bound to the Thermus thermophilus ribosome with a P-site tRNA at 2.9 angstroms resolution. The C-terminal domain of EF4 reaches into the peptidyl transferase center and interacts with the acceptor stem of the peptidyl-tRNA in the P site. The ribosome is in an unusual state of ratcheting with the 30S subunit rotated clockwise relative to the 50S subunit, resulting in a remodeled decoding center. The structure is consistent with EF4 functioning either as a back-translocase or a ribosome sequester.

Original languageEnglish (US)
Pages (from-to)684-687
Number of pages4
JournalScience
Volume345
Issue number6197
DOIs
StatePublished - Aug 8 2014
Externally publishedYes

ASJC Scopus subject areas

  • General

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