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Ribosome-induced ch...
Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis
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- Villa, Elizabeth (author)
- Beckman Institute, University of Illinois at Urbana-Champaign, Urbana, IL
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- Sengupta, Jayati (author)
- Wadsworth Center, Albany, NY
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- Trabuco, Leonardo G. (author)
- Beckman Institute, University of Illinois at Urbana-Champaign, Urbana, IL
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- LeBarron, Jamie (author)
- Wadsworth Center, Albany, NY
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Baxter, William T. (author)
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- Shaikh, Tanvir R. (author)
- Wadsworth Center, Albany, NY
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- Grassucci, Robert A. (author)
- Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY
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- Nissen, Poul (author)
- Department of Molecular Biology, University of Aarhus, Aarhus, Denmark
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- Ehrenberg, Måns (author)
- Uppsala universitet,Molekylärbiologi,ehrenberg
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- Schulten, Klaus (author)
- Beckman Institute, University of Illinois at Urbana-Champaign, Urbana, IL
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- Frank, Joachim (author)
- Department of Biological Sciences, Columbia University, New York, NY
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(creator_code:org_t)
- 2009-01-27
- 2009
- English.
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In: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 0027-8424 .- 1091-6490. ; 106:4, s. 1063-1068
- Related links:
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http://www.pnas.org/...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Subject headings
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Keyword
- cryo-EM
- Decoding
- Flexible fitting
- GTPase
- Ternary complex
- Biology
- Biologi
- Molecular Biology
- Molekylärbiologi
Publication and Content Type
- ref (subject category)
- art (subject category)
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- By the author/editor
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Villa, Elizabeth
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Sengupta, Jayati
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Trabuco, Leonard ...
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LeBarron, Jamie
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Baxter, William ...
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Shaikh, Tanvir R ...
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show more...
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Grassucci, Rober ...
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Nissen, Poul
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Ehrenberg, Måns
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Schulten, Klaus
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Frank, Joachim
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show less...
- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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Proceedings of t ...
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Uppsala University