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

29 Citations (Scopus)

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

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Peptide Elongation Factors
Ribosomes
Guanosine
Transfer RNA
Peptide Elongation Factor G
Peptidyl Transferases
Thermus thermophilus
Diphosphates
Proteins

ASJC Scopus subject areas

  • General

Cite this

Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome. / Gagnon, Matthieu; Lin, Jinzhong; Bulkley, David; Steitz, Thomas A.

In: Science, Vol. 345, No. 6197, 08.08.2014, p. 684-687.

Research output: Contribution to journalArticle

Gagnon, Matthieu ; Lin, Jinzhong ; Bulkley, David ; Steitz, Thomas A. / Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome. In: Science. 2014 ; Vol. 345, No. 6197. pp. 684-687.
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