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Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis
Beckman Institute, University of Illinois at Urbana-Champaign, Urbana, IL.
Wadsworth Center, Albany, NY.
Beckman Institute, University of Illinois at Urbana-Champaign, Urbana, IL.
Wadsworth Center, Albany, NY.
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2009 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 106, no 4, 1063-1068 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2009. Vol. 106, no 4, 1063-1068 p.
Keyword [en]
cryo-EM, Decoding, Flexible fitting, GTPase, Ternary complex
National Category
Biological Sciences
Research subject
Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-104043DOI: 10.1073/pnas.0811370106ISI: 000262831600021PubMedID: 19122150OAI: oai:DiVA.org:uu-104043DiVA: diva2:219289
Available from: 2009-05-27 Created: 2009-05-27 Last updated: 2011-03-10Bibliographically approved

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