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Structural Biophysics Laboratory (SBL)
Protein-Nucleic Acid Interaction Section

Research Projects: The dynamics and structure of ribosome protein L11

Peptidyl-transferase on the 70S Ribosome

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.

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