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Three‐dimensional cryo‐electron microscopy localization of EF2 in the Saccharomyces cerevisiae 80S ribosome at 17.5 Å resolution
Author(s) -
GomezLorenzo Maria G.,
Spahn Christian M.T.,
Agrawal Rajendra K.,
Grassucci Robert A.,
Penczek Pawel,
Chakraburtty Kalpana,
Ballesta Juan P.G.,
Lavandera Jose L.,
GarciaBustos Jose F.,
Frank Joachim
Publication year - 2000
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/19.11.2710
Subject(s) - biology , saccharomyces cerevisiae , electron microscope , cryo electron microscopy , resolution (logic) , ribosome , microscopy , biophysics , microbiology and biotechnology , computational biology , yeast , genetics , optics , rna , physics , gene , artificial intelligence , computer science
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.