{"id":{"repo_id":"lethbridge","oai_identifier":"oai:opus.uleth.ca:10133/3465"},"canonical_url":"https://search.dev.ndltd.org/etd/lethbridge/oai:opus.uleth.ca:10133/3465","repository":{"repo_id":"lethbridge","name":"University of Lethbridge","base_url":"https://opus.uleth.ca/server/oai/request"},"display":{"title":"Structural dynamics of elongation factor Tu","abstract":"Elongation Factor (EF) Tu is universally conserved and delivers aminoacyl-tRNAs (aatRNAs) to the ribosome. To perform this essential task, EF-Tu binds aa-tRNA in an active GTP-bound state, and GTP hydrolysis is critical for deposition of aa-tRNA into the ribosome. Following each aa-tRNA delivery, nucleotide exchange is required for reactivation of EF-Tu•GDP to EF-Tu•GTP. EF-Tu undergoes a variety of conformational changes during each round of aa-tRNA delivery and reactivation. Here, molecular dynamics simulations in silico and kinetic measurements in vitro demonstrate that structural dynamics of EF-Tu on the sub-nanosecond timescale are correlated with EF-Tu functions on the timescale of seconds. Specifically, structural dynamics of the conserved P-loop and switch II regions are important for nucleotide binding in EF-Tu. Additionally, interactions between domain II of EF-Tu and the small ribosomal subunit, which stimulate GTP hydrolysis on EF-Tu, have the potential to regulate structural dynamics of switch I and switch II.","abstract_html":"Elongation Factor (EF) Tu is universally conserved and delivers aminoacyl-tRNAs (aatRNAs) to the ribosome. To perform this essential task, EF-Tu binds aa-tRNA in an active GTP-bound state, and GTP hydrolysis is critical for deposition of aa-tRNA into the ribosome. Following each aa-tRNA delivery, nucleotide exchange is required for reactivation of EF-Tu•GDP to EF-Tu•GTP. EF-Tu undergoes a variety of conformational changes during each round of aa-tRNA delivery and reactivation. Here, molecular dynamics simulations in silico and kinetic measurements in vitro demonstrate that structural dynamics of EF-Tu on the sub-nanosecond timescale are correlated with EF-Tu functions on the timescale of seconds. Specifically, structural dynamics of the conserved P-loop and switch II regions are important for nucleotide binding in EF-Tu. Additionally, interactions between domain II of EF-Tu and the small ribosomal subunit, which stimulate GTP hydrolysis on EF-Tu, have the potential to regulate structural dynamics of switch I and switch II.","abstract_has_math":false,"creators":["Mercier, Evan A."],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2013,"date_issued":"2013","date_published":"2013","updated_at":"2026-07-27T20:02:41Z","subjects":["Genetic translation -- Research","Aminoacyl-tRNA -- Research","G proteins -- Research","Dissertations, Academic"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["hdl:10133/3465"],"render_values":[{"text":"hdl:10133/3465","href":null,"code":true}]}]},"links":{"outbound_url":null,"outbound_label":null,"outbound_source":null},"metadata_groups":[{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.issued","label":"Date","values":["2013"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Genetic translation -- Research","Aminoacyl-tRNA -- Research","G proteins -- Research","Dissertations, Academic"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["hdl:10133/3465"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.other","label":"Dc Description Other","values":["Elongation Factor (EF) Tu is universally conserved and delivers aminoacyl-tRNAs (aatRNAs) to the ribosome. To perform this essential task, EF-Tu binds aa-tRNA in an active GTP-bound state, and GTP hydrolysis is critical for deposition of aa-tRNA into the ribosome. Following each aa-tRNA delivery, nucleotide exchange is required for reactivation of EF-Tu•GDP to EF-Tu•GTP. EF-Tu undergoes a variety of conformational changes during each round of aa-tRNA delivery and reactivation. Here, molecular dynamics simulations in silico and kinetic measurements in vitro demonstrate that structural dynamics of EF-Tu on the sub-nanosecond timescale are correlated with EF-Tu functions on the timescale of seconds. Specifically, structural dynamics of the conserved P-loop and switch II regions are important for nucleotide binding in EF-Tu. Additionally, interactions between domain II of EF-Tu and the small ribosomal subunit, which stimulate GTP hydrolysis on EF-Tu, have the potential to regulate structural dynamics of switch I and switch II."]},{"key":"dc:title","label":"Title","values":["Structural dynamics of elongation factor Tu"]}]}],"canonical_facts":{"dc:date.issued":["2013"],"dc:description.other":["Elongation Factor (EF) Tu is universally conserved and delivers aminoacyl-tRNAs (aatRNAs) to the ribosome. To perform this essential task, EF-Tu binds aa-tRNA in an active GTP-bound state, and GTP hydrolysis is critical for deposition of aa-tRNA into the ribosome. Following each aa-tRNA delivery, nucleotide exchange is required for reactivation of EF-Tu•GDP to EF-Tu•GTP. EF-Tu undergoes a variety of conformational changes during each round of aa-tRNA delivery and reactivation. Here, molecular dynamics simulations in silico and kinetic measurements in vitro demonstrate that structural dynamics of EF-Tu on the sub-nanosecond timescale are correlated with EF-Tu functions on the timescale of seconds. Specifically, structural dynamics of the conserved P-loop and switch II regions are important for nucleotide binding in EF-Tu. Additionally, interactions between domain II of EF-Tu and the small ribosomal subunit, which stimulate GTP hydrolysis on EF-Tu, have the potential to regulate structural dynamics of switch I and switch II."],"dc:identifier":["hdl:10133/3465"],"dc:subject":["Genetic translation -- Research","Aminoacyl-tRNA -- Research","G proteins -- Research","Dissertations, Academic"],"dc:title":["Structural dynamics of elongation factor Tu"],"dc:type":["Thesis"]},"updated_at":"2026-07-27T20:02:41Z"}