Conformational changes of elongation factor g on the ribosome during tRNA translocation

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

Research output: Contribution to journalArticle

61 Citations (Scopus)

Abstract

The universally conserved GTPase elongation factor G (EF-G) catalyzes the translocation of tRNA and mRNA on the ribosome after peptide bond formation. Despite numerous studies suggesting that EF-G undergoes extensive conformational rearrangements during translocation, high-resolution structures exist for essentially only one conformation of EF-G in complex with the ribosome. Here, we report four atomic-resolution crystal structures of EF-G bound to the ribosome programmed in the pre- and posttranslocational states and to the ribosome trapped by the antibiotic dityromycin. We observe a previously unseen conformation of EF-G in the pretranslocation complex, which is independently captured by dityromycin on the ribosome. Our structures provide insights into the conformational space that EF-G samples on the ribosome and reveal that tRNA translocation on the ribosome is facilitated by a structural transition of EF-G from a compact to an elongated conformation, which can be prevented by the antibiotic dityromycin.

Original languageEnglish (US)
Pages (from-to)219-227
Number of pages9
JournalCell
Volume160
Issue number1-2
DOIs
StatePublished - Jan 15 2015
Externally publishedYes

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Peptide Elongation Factor G
Peptide Elongation Factors
Transfer RNA
Ribosomes
Conformations
Anti-Bacterial Agents
GTP Phosphohydrolases
Crystal structure
Messenger RNA
Peptides

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Conformational changes of elongation factor g on the ribosome during tRNA translocation. / Lin, Jinzhong; Gagnon, Matthieu; Bulkley, David; Steitz, Thomas A.

In: Cell, Vol. 160, No. 1-2, 15.01.2015, p. 219-227.

Research output: Contribution to journalArticle

Lin, Jinzhong ; Gagnon, Matthieu ; Bulkley, David ; Steitz, Thomas A. / Conformational changes of elongation factor g on the ribosome during tRNA translocation. In: Cell. 2015 ; Vol. 160, No. 1-2. pp. 219-227.
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