title: Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha.
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.
authors: Institute of Molecular and Structural Biology University of Aarhus Gustav Wieds Vej 10C DK8000, Arhus, Denmark.
authors: G R
authors: GR
authors: Andersen
authors: L
authors: L
authors: Pedersen
authors: L
authors: L
authors: Valente
authors: I
authors: I
authors: Chatterjee
authors: T G
authors: TG
authors: Kinzy
authors: M
authors: M
authors: Kjeldgaard
authors: J
authors: J
authors: Nyborg
mesh_terms: D001665:Binding Sites; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D008274:Magnesium / Q000378:metabolism; D008958:Models, Molecular; D009711:Nucleotides / Q000235:genetics / Q000378:metabolism*; D020648:Peptide Elongation Factor 1 / Q000737:chemistry* / Q000378:metabolism*; D010444:Peptide Elongation Factor Tu / Q000737:chemistry / Q000378:metabolism; D018583:Pliability; D014176:Protein Biosynthesis; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012343:RNA, Transfer / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship
chemical_list: D009711:Nucleotides; D020648:Peptide Elongation Factor 1; D029701:Saccharomyces cerevisiae Proteins; D012343:RNA, Transfer; D010444:Peptide Elongation Factor Tu; D008274:Magnesium