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

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  • Bioinformatics Research Centre (BiRC)
  • Interdisciplinary Nanoscience Center
  • Department of Molecular Biology
  • Department of Molecular Biology
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.
Original languageEnglish
JournalScience
Volume270
Issue5241
Pages (from-to)1464-72
Number of pages8
ISSN0036-8075
Publication statusPublished - 1995

    Research areas

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

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