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

@article{citeulike:4258975, 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 = {Villa, E. and Sengupta, J. and Trabuco, L. G. and LeBarron, J. and Baxter, W. T. and Shaikh, T. R. and Grassucci, R. A. and Nissen, P. and Ehrenberg, M. and Schulten, K. and Frank, J.}, citeulike-article-id = {4258975}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.0811370106}, citeulike-linkout-1 = {http://www.pnas.org/content/106/4/1063.full.abstract}, citeulike-linkout-2 = {http://www.pnas.org/content/106/4/1063.full.full.pdf}, citeulike-linkout-3 = {http://view.ncbi.nlm.nih.gov/pubmed/19122150}, citeulike-linkout-4 = {http://www.hubmed.org/display.cgi?uids=19122150}, day = {27}, doi = {10.1073/pnas.0811370106}, issn = {1091-6490}, journal = {Proceedings of the National Academy of Sciences of the United States of America}, keywords = {allostery, em, protein, ribosome, structure}, month = {January}, number = {4}, pages = {1063--1068}, posted-at = {2009-04-03 08:13:23}, priority = {2}, title = {Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis.}, url = {http://dx.doi.org/10.1073/pnas.0811370106}, volume = {106}, year = {2009} }

TY - JOUR ID - citeulike:4258975 L3 - citeulike-article-id:4258975 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. IS - 4 JF - Proceedings of the National Academy of Sciences of the United States of America SN - 1091-6490 EP - 1068 TI - Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis. VL - 106 SP - 1063 KW - allostery KW - em KW - protein KW - ribosome KW - structure AU - Villa, E AU - Sengupta, J AU - Trabuco, LG AU - LeBarron, J AU - Baxter, WT AU - Shaikh, TR AU - Grassucci, RA AU - Nissen, P AU - Ehrenberg, M AU - Schulten, K AU - Frank, J PY - 2009/01/27/ UR - http://dx.doi.org/10.1073/pnas.0811370106 ER -