The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution

Nature. 1996 Feb 8;379(6565):511-8. doi: 10.1038/379511a0.


The crystal structure of the EF-Tu.EF-Ts complex from Escherichia coli has been determined to a resolution of 2.5 A. The complex contains two subunits of each of the elongation factors. The two EF-Ts molecules form a tight dimer, but there is little contact between the two EF-Tu molecules. The interaction of EF-Ts with EF-Tu results principally in the disruption of the Mg2+ ion binding site, thereby reducing the affinity of EF-Tu for guanine nucleotides.

MeSH terms

  • Amino Acid Sequence
  • Crystallography, X-Ray
  • Escherichia coli / chemistry*
  • Guanosine Diphosphate / chemistry
  • Magnesium / chemistry
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Elongation Factor Tu / chemistry*
  • Peptide Elongation Factors / chemistry*
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Secondary


  • Peptide Elongation Factors
  • elongation factor Ts
  • Guanosine Diphosphate
  • Peptide Elongation Factor Tu
  • Magnesium