Open Access. Powered by Scholars. Published by Universities.®
Articles 1 - 1 of 1
Full-Text Articles in Physics
E. Coli Elongation Factor Tu Bound To A Gtp Analogue Displays An Open Conformation Equivalent To The Gdp-Bound Form, Jesper S. Johansen, Darius Kavaliauskas, Shawn H. Pfeil, Mickael Blaise, Barry C. Cooperman, Yale E. Goldman, Søren S. Thirup, Charlotte R. Knudsen
E. Coli Elongation Factor Tu Bound To A Gtp Analogue Displays An Open Conformation Equivalent To The Gdp-Bound Form, Jesper S. Johansen, Darius Kavaliauskas, Shawn H. Pfeil, Mickael Blaise, Barry C. Cooperman, Yale E. Goldman, Søren S. Thirup, Charlotte R. Knudsen
Physics & Engineering Faculty Publications
According to the traditional view, GTPases act as molecular switches, which cycle between distinct ‘on’ and ‘off’ conformations bound to GTP and GDP, respectively. Translation elongation factor EF-Tu is a GTPase essential for prokaryotic protein synthesis. In its GTP-bound form, EF-Tu delivers aminoacylated tRNAs to the ribosome as a ternary complex. GTP hydrolysis is thought to cause the release of EF-Tu from aminoacyl-tRNA and the ribosome due to a dramatic conformational change following Pi release. Here, the crystal structure of Escherichia coli EF-Tu in complex with a non-hydrolysable GTP analogue (GDPNP) has been determined. Remarkably, the overall conformation of EF-Tu·GDPNP …