Ternary Complex of EF-Tu and Its Action on the Ribosome

TL;DRAbstract

This chapter describes the advances made in the structural studies of elongation factor EF-Tu during the last decade, and shows that the structural transition between the active, aa-tRNA binding form and the inactive form of EF-Tu is surprisingly large. Most of the various functional states of EF-Tu have been illustrated by structural results over the last few years. Very recently the authors had finished the refinement of the structure of bovine mitochondrial EF-Tu·GDP at a resolution of 1.94 Å in a collaboration with Linda Spremulli, University of North Carolina. The modes by which EF-G and the ternary complex of EF-Tu interact with the ribosome have been elegantly demonstrated by cryo-electron microscopy (EM) reconstructions. The structure of the ternary complex on the ribosome is blocked with kirromycin. The mechanism of the GTPase reaction of EF-Tu has been exceedingly difficult to pin down. The nucleotide exchange mechanism of EF-Ts is not well understood in structural terms. We

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