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

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Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis. / Villa, Elizabeth; Sengupta, Jayati; Trabuco, Leonard G.; Lebarron, J; Baxter, W. T.; Shaikh, T. R.; Grasucci, R. A.; Nissen, Poul; Ehrenberg, Måns; Schulten, Klaus; Joachim, Frank.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 106, No. 1, 02.01.2009, p. 1063-1068.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Villa, E, Sengupta, J, Trabuco, LG, Lebarron, J, Baxter, WT, Shaikh, TR, Grasucci, RA, Nissen, P, Ehrenberg, M, Schulten, K & Joachim, F 2009, 'Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis', Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 1, pp. 1063-1068.

APA

Villa, E., Sengupta, J., Trabuco, L. G., Lebarron, J., Baxter, W. T., Shaikh, T. R., Grasucci, R. A., Nissen, P., Ehrenberg, M., Schulten, K., & Joachim, F. (2009). Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis. Proceedings of the National Academy of Sciences of the United States of America, 106(1), 1063-1068.

CBE

Villa E, Sengupta J, Trabuco LG, Lebarron J, Baxter WT, Shaikh TR, Grasucci RA, Nissen P, Ehrenberg M, Schulten K, Joachim F. 2009. Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis. Proceedings of the National Academy of Sciences of the United States of America. 106(1):1063-1068.

MLA

Villa, Elizabeth et al. "Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis". Proceedings of the National Academy of Sciences of the United States of America. 2009, 106(1). 1063-1068.

Vancouver

Villa E, Sengupta J, Trabuco LG, Lebarron J, Baxter WT, Shaikh TR et al. Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis. Proceedings of the National Academy of Sciences of the United States of America. 2009 Jan 2;106(1):1063-1068.

Author

Villa, Elizabeth ; Sengupta, Jayati ; Trabuco, Leonard G. ; Lebarron, J ; Baxter, W. T. ; Shaikh, T. R. ; Grasucci, R. A. ; Nissen, Poul ; Ehrenberg, Måns ; Schulten, Klaus ; Joachim, Frank. / Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis. In: Proceedings of the National Academy of Sciences of the United States of America. 2009 ; Vol. 106, No. 1. pp. 1063-1068.

Bibtex

@article{b6cd1cd0faf511dd8f9a000ea68e967b,
title = "Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis",
abstract = "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.",
author = "Elizabeth Villa and Jayati Sengupta and Trabuco, {Leonard G.} and J Lebarron and Baxter, {W. T.} and Shaikh, {T. R.} and Grasucci, {R. A.} and Poul Nissen and M{\aa}ns Ehrenberg and Klaus Schulten and Frank Joachim",
year = "2009",
month = jan,
day = "2",
language = "English",
volume = "106",
pages = "1063--1068",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "1",

}

RIS

TY - JOUR

T1 - Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis

AU - Villa, Elizabeth

AU - Sengupta, Jayati

AU - Trabuco, Leonard G.

AU - Lebarron, J

AU - Baxter, W. T.

AU - Shaikh, T. R.

AU - Grasucci, R. A.

AU - Nissen, Poul

AU - Ehrenberg, Måns

AU - Schulten, Klaus

AU - Joachim, Frank

PY - 2009/1/2

Y1 - 2009/1/2

N2 - 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.

AB - 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.

M3 - Journal article

VL - 106

SP - 1063

EP - 1068

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 1

ER -