Structural Basis for Nucleotide Exchange and Competition with tRNA in the Yeast Elongation Factor Complex eEF1A:eEF1Bα

Document Type

Article

Publication Title

Molecular Cell

Publication Date

11-2000

Abstract

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.

Comments

This article was originally published as Andersen, G.R. Pedersen, L., Valente, L., Chatterjee, I., Kinzy, T.G., Kjeldegard, M. and Nyborg, J. (2000) Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Bï¡ï€¬ï€ Molecular Cell 6: 1261-1266. PMID: 11106763

DOI

10.1016/S1097-2765(00)00122-2

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