Protein-Nucleic Acid Interaction Section
Research Projects: The dynamics and structure of ribosome protein L11
Our group has long been interested in biochemical and biological events involved
in translation and post-translation processes. The L11 binding site is one of the
most important functional sites in the ribosome. The N-terminal domain of L11 has
been implicated as a “reversible switch” in facilitating the coordinated movements
associated with EF-G-driven GTP hydrolysis. The reversible switch mechanism has
been hypothesized to require conformational flexibility involving re-orientation
and re-positioning of the two L11 domains, and warrants a close examination of the
structure and dynamics of L11.
Lee D, Walsh JD, Yu P, Markus MA, Choli-Papadopoulou T, Schwieters CD,
Krueger S, Draper DE, Wang YX.
The structure of free L11 and functional dynamics of L11 in free, L11-rRNA(58 nt)
binary and L11-rRNA(58 nt)-thiostrepton ternary complexes.
J Mol Biol. 367: 1007-22, 2007.