Three-dimensional cryo-electron microscopy localization of EF2 in the Saccharomyces cerevisiae 80S ribosome at 17.5 Å resolution

Maria G. Gomez-Lorenzo, Christian M.T. Spahn, Rajendra K. Agrawal, Robert A. Grassucci, Pawel Penczek, Kalpana Chakraburtty, Juan P.G. Ballesta, Jose L. Lavandera, Jose F. Garcia-Bustos, Joachim Frank

Research output: Contribution to journalArticleResearchpeer-review

142 Citations (Scopus)

Abstract

Using a sordarin derivative, an antifungal drug, it was possible to determine the structure of a eukaryotic ribosome·EF2 complex at 17.5 Å resolution by three-dimensional (3D) cryo-electron microscopy. EF2 is directly visible in the 3D map and the overall arrangement of the complex from Saccharomyces cerevisiae corresponds to that previously seen in Escherichia coli. However, pronounced differences were found in two prominent regions. First, in the yeast system the interaction between the elongation factor and the stalk region of the large subunit is much more extensive. Secondly, domain IV of EF2 contains additional mass that appears to interact with the head of the 40S subunit and the region of the main bridge of the 60S subunit. The shape and position of domain IV of EF2 suggest that it might interact directly with P-site-bound tRNA.

Original languageEnglish
Pages (from-to)2710-2718
Number of pages9
JournalThe EMBO Journal
Volume19
Issue number11
Publication statusPublished - 1 Jun 2000
Externally publishedYes

Keywords

  • Elongation
  • GM193663
  • Sordarin
  • Translation
  • Yeast

Cite this