Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha.
Mol Cell, 2000/11;6(5):1261-6.
Andersen GR[1], Pedersen L, Valente L, Chatterjee I, Kinzy TG, Kjeldgaard M, Nyborg J
Affiliations
PMID: 11106763
Impact factor: 19.328
Abstract
The crystal structure of a complex between the protein biosynthesis elongation factor eEF1A (formerly EF-1alpha) and the catalytic C terminus of its exchange factor, eEF1Balpha (formerly EF-1beta), was determined to 1.67 A 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 Mg(2+) ion associated with the nucleotide. The second end of eEF1Balpha 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 eEF1Balpha and aminoacylated tRNA may be a central element in channeling the reactants in eukaryotic protein synthesis. The recognition of eEF1A by eEF1Balpha 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.
MeSH terms
Binding Sites; Conserved Sequence; Crystallography, X-Ray; Magnesium; Models, Molecular; Nucleotides; Peptide Elongation Factor 1; Peptide Elongation Factor Tu; Pliability; Protein Biosynthesis; Protein Structure, Secondary; Protein Structure, Tertiary; RNA, Transfer; Saccharomyces cerevisiae Proteins; Structure-Activity Relationship
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