Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha

Mol Cell. 2000 Nov;6(5):1261-6. doi: 10.1016/s1097-2765(00)00122-2.


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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Binding Sites
  • Conserved Sequence
  • Crystallography, X-Ray
  • Magnesium / metabolism
  • Models, Molecular
  • Nucleotides / genetics
  • Nucleotides / metabolism*
  • Peptide Elongation Factor 1 / chemistry*
  • Peptide Elongation Factor 1 / metabolism*
  • Peptide Elongation Factor Tu / chemistry
  • Peptide Elongation Factor Tu / metabolism
  • Pliability
  • Protein Biosynthesis*
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • RNA, Transfer / chemistry
  • RNA, Transfer / genetics
  • RNA, Transfer / metabolism*
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / metabolism
  • Structure-Activity Relationship


  • Nucleotides
  • Peptide Elongation Factor 1
  • Saccharomyces cerevisiae Proteins
  • RNA, Transfer
  • Peptide Elongation Factor Tu
  • Magnesium

Associated data

  • PDB/1F60