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Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis

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  • Elizabeth Villa, University of Illinois at Urbana-Champaign, United States
  • Jayati Sengupta, India
  • Leonard G. Trabuco, University of Illinois at Urbana-Champaign, United States
  • J Lebarron, United States
  • W. T. Baxter, United States
  • T. R. Shaikh, United States
  • R. A. Grasucci, United States
  • Poul Nissen
  • Måns Ehrenberg, Uppsala University, Sweden
  • Klaus Schulten, University of Illinois at Urbana-Champaign, United States
  • Frank Joachim, Columbia University, United States
  • Department of Molecular Biology
In translation, elongation factor Tu (EF-Tu) molecules deliver aminoacyl-tRNAs to the mRNA-programmed ribosome. The GTPase activity of EF-Tu is triggered by ribosome-induced conformational changes of the factor that play a pivotal role in the selection of the cognate aminoacyl-tRNAs. We present a 6.7-A cryo-electron microscopy map of the aminoacyl-tRNA x EF-Tu x GDP x kirromycin-bound Escherichia coli ribosome, together with an atomic model of the complex obtained through molecular dynamics flexible fitting. The model reveals the conformational changes in the conserved GTPase switch regions of EF-Tu that trigger hydrolysis of GTP, along with key interactions, including those between the sarcin-ricin loop and the P loop of EF-Tu, and between the effector loop of EF-Tu and a conserved region of the 16S rRNA. Our data suggest that GTP hydrolysis on EF-Tu is controlled through a hydrophobic gate mechanism.
Original languageEnglish
JournalProceedings of the National Academy of Sciences of the United States of America
Volume106
Issue1
Pages (from-to)1063-1068
ISSN0027-8424
Publication statusPublished - 2 Jan 2009

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