Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog

Science. 1995 Dec 1;270(5241):1464-72. doi: 10.1126/science.270.5241.1464.


The structure of the ternary complex consisting of yeast phenylalanyl-transfer RNA (Phe-tRNAPhe), Thermus aquaticus elongation factor Tu (EF-Tu), and the guanosine triphosphate (GTP) analog GDPNP was determined by x-ray crystallography at 2.7 angstrom resolution. The ternary complex participates in placing the amino acids in their correct order when messenger RNA is translated into a protein sequence on the ribosome. The EF-Tu-GDPNP component binds to one side of the acceptor helix of Phe-tRNAPhe involving all three domains of EF-Tu. Binding sites for the phenylalanylated CCA end and the phosphorylated 5' end are located at domain interfaces, whereas the T stem interacts with the surface of the beta-barrel domain 3. The binding involves many conserved residues in EF-Tu. The overall shape of the ternary complex is similar to that of the translocation factor, EF-G-GDP, and this suggests a novel mechanism involving "molecular mimicry" in the translational apparatus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anticodon
  • Base Sequence
  • Binding Sites
  • Crystallography, X-Ray
  • Guanosine Diphosphate / chemistry
  • Guanosine Diphosphate / metabolism
  • Guanosine Triphosphate / analogs & derivatives*
  • Guanosine Triphosphate / chemistry
  • Guanosine Triphosphate / metabolism
  • Histidine / metabolism
  • Lysine / metabolism
  • Models, Molecular
  • Molecular Mimicry
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Peptide Elongation Factor G
  • Peptide Elongation Factor Tu / chemistry*
  • Peptide Elongation Factor Tu / metabolism
  • Peptide Elongation Factors / chemistry
  • Peptide Elongation Factors / metabolism
  • Peptide Initiation Factors / chemistry
  • Peptide Initiation Factors / metabolism
  • Peptide Termination Factors / chemistry
  • Peptide Termination Factors / metabolism
  • Prokaryotic Initiation Factor-2
  • Protein Biosynthesis
  • Protein Conformation
  • Protein Structure, Secondary
  • RNA, Transfer, Amino Acyl / chemistry*
  • RNA, Transfer, Amino Acyl / metabolism
  • Ribosomes / metabolism
  • Thermus


  • Anticodon
  • Peptide Elongation Factor G
  • Peptide Elongation Factors
  • Peptide Initiation Factors
  • Peptide Termination Factors
  • Prokaryotic Initiation Factor-2
  • RNA, Transfer, Amino Acyl
  • Guanosine Diphosphate
  • Histidine
  • Guanosine Triphosphate
  • Peptide Elongation Factor Tu
  • Lysine