Structural dynamics of elongation factor Tu
Date
2013
Authors
Mercier, Evan A.
Journal Title
Journal ISSN
Volume Title
Publisher
Lethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistry
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.
Description
xii, 235 leaves : ill. (some col.) ; 29 cm
Keywords
Genetic translation -- Research , Aminoacyl-tRNA -- Research , G proteins -- Research , Dissertations, Academic