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Proc Natl Acad Sci U S A. 2011 Jun 14;108(24):9827-32. doi: 10.1073/pnas.1105714108. Epub 2011 May 26.

Converting structural information into an allosteric-energy-based picture for elongation factor Tu activation by the ribosome.

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  • 1Department of Chemistry, 418 Seeley G Mudd Building, University of Southern California, 3620 McClintock Avenue, Los Angeles, CA 90089-1062, USA.


The crucial process of aminoacyl-tRNA delivery to the ribosome is energized by the GTPase reaction of the elongation factor Tu (EF-Tu). Advances in the elucidation of the structure of the EF-Tu/ribosome complex provide the rare opportunity of gaining a detailed understanding of the activation process of this system. Here, we use quantitative simulation approaches and reproduce the energetics of the GTPase reaction of EF-Tu with and without the ribosome and with several key mutants. Our study provides a novel insight into the activation process. It is found that the critical H84 residue is not likely to behave as a general base but rather contributes to an allosteric effect, which includes a major transition state stabilization by the electrostatic effect of the P loop and other regions of the protein. Our findings have general relevance to GTPase activation, including the processes that control signal transduction.

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