Structural Basis for Nucleotide Exchange and Competition with tRNA in the Yeast Elongation Factor Complex eEF1A:eEF1Bα
The crystal structure of a complex between the protein biosynthesis elongation factor eEF1A (formerly EF-1α) and the catalytic C terminus of its exchange factor, eEF1Bα (formerly EF-1β), was determined to 1.67 Å resolution. One end of the nucleotide exchange factor is buried between the switch 1 and 2 regions of eEF1A and destroys the binding site for the Mg2+ ion associated with the nucleotide. The second end of eEF1Bα interacts with domain 2 of eEF1A in the region hypothesized to be involved in the binding of the CCA-aminoacyl end of the tRNA. The competition between eEF1Bα and aminoacylated tRNA may be a central element in channeling the reactants in eukaryotic protein synthesis. The recognition of eEF1A by eEF1Bα is very different from that observed in the prokaryotic EF-Tu:EF-Ts complex. Recognition of the switch 2 region in nucleotide exchange is, however, common to the elongation factor complexes and those of Ras:Sos and Arf1:Sec7.
Andersen, Gregers Rom; Pederson, Lise; Valente, Louis; Chatterjee, Ishita; Kinzy, Terri Goss; Kjeldgaard, Morten; and Nyborg, Jens, "Structural Basis for Nucleotide Exchange and Competition with tRNA in the Yeast Elongation Factor Complex eEF1A:eEF1Bα" (2000). Faculty Publications – Biological Sciences. 108.