<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Villa, Elizabeth</style></author><author><style face="normal" font="default" size="100%">Sengupta, Jayati</style></author><author><style face="normal" font="default" size="100%">Trabuco, Leonardo G</style></author><author><style face="normal" font="default" size="100%">LeBarron, Jamie</style></author><author><style face="normal" font="default" size="100%">Baxter, Bill</style></author><author><style face="normal" font="default" size="100%">Shaikh, Tanvir R</style></author><author><style face="normal" font="default" size="100%">Grassucci, Robert A</style></author><author><style face="normal" font="default" size="100%">Nissen, Poul</style></author><author><style face="normal" font="default" size="100%">Ehrenberg, Måns</style></author><author><style face="normal" font="default" size="100%">Schulten, Klaus</style></author><author><style face="normal" font="default" size="100%">Frank, Joachim</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis.</style></title><secondary-title><style face="normal" font="default" size="100%">Proc Natl Acad Sci U S A</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Proc. Natl. Acad. Sci. U.S.A.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Cryoelectron Microscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Enzyme Activation</style></keyword><keyword><style  face="normal" font="default" size="100%">Escherichia coli</style></keyword><keyword><style  face="normal" font="default" size="100%">Escherichia coli Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Guanosine Triphosphate</style></keyword><keyword><style  face="normal" font="default" size="100%">Histidine</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrolysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrophobic and Hydrophilic Interactions</style></keyword><keyword><style  face="normal" font="default" size="100%">Models, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Peptide Elongation Factor Tu</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Structure, Secondary</style></keyword><keyword><style  face="normal" font="default" size="100%">Ribosomal Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Ribosomes</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Transfer</style></keyword><keyword><style  face="normal" font="default" size="100%">Signal Transduction</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">01/2009</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/19122150</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">106</style></volume><pages><style face="normal" font="default" size="100%">1063-8</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;span style=&quot;font-family: arial, helvetica, clean, sans-serif; font-size: 13px; line-height: 17px;&quot;&gt;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.&lt;/span&gt;&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Shaikh, Tanvir R</style></author><author><style face="normal" font="default" size="100%">Gao, Haixiao</style></author><author><style face="normal" font="default" size="100%">Baxter, Bill</style></author><author><style face="normal" font="default" size="100%">Asturias, Francisco J</style></author><author><style face="normal" font="default" size="100%">Boisset, Nicolas</style></author><author><style face="normal" font="default" size="100%">Leith, ArDean</style></author><author><style face="normal" font="default" size="100%">Frank, Joachim</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs.</style></title><secondary-title><style face="normal" font="default" size="100%">Nat Protoc</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Nat Protoc</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Image Processing, Computer-Assisted</style></keyword><keyword><style  face="normal" font="default" size="100%">Microscopy, Electron</style></keyword><keyword><style  face="normal" font="default" size="100%">Models, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Structure</style></keyword><keyword><style  face="normal" font="default" size="100%">Software</style></keyword><keyword><style  face="normal" font="default" size="100%">User-Computer Interface</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2008</style></year><pub-dates><date><style  face="normal" font="default" size="100%">10/2008</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/19180078</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">3</style></volume><pages><style face="normal" font="default" size="100%">1941-74</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;span style=&quot;font-family: arial, helvetica, clean, sans-serif; font-size: 13px; line-height: 17px;&quot;&gt;This protocol describes the reconstruction of biological molecules from the electron micrographs of single particles. Computation here is performed using the image-processing software SPIDER and can be managed using a graphical user interface, termed the SPIDER Reconstruction Engine. Two approaches are described to obtain an initial reconstruction: random-conical tilt and common lines. Once an existing model is available, reference-based alignment can be used, a procedure that can be iterated. Also described is supervised classification, a method to look for homogeneous subsets when multiple known conformations of the molecule may coexist.&lt;/span&gt;&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">12</style></issue></record></records></xml>