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

• Published in: Science (American Association for the Advancement of Science) 1995-12, Vol.270 (5241), p.1464-1472
• Main Authors: NISSEN, P, KJELDGAARD, M, THIRUP, S, POLEKHINA, G, RESHETNIKOVA, L, CLARK, B. F. C, NYBORG, J
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Anticodon; Base Sequence; Binding Sites; Biological and medical sciences; Crystalline structure; Crystallography; Crystallography, X-Ray; Fundamental and applied biological sciences. Psychology; Guanosine Diphosphate - chemistry; Guanosine Diphosphate - metabolism; Guanosine Triphosphate - analogs & derivatives; Guanosine Triphosphate - chemistry; Guanosine Triphosphate - metabolism; Histidine - metabolism; Lysine - metabolism; Models, Molecular; Molecular and cellular biology; Molecular biophysics; Molecular genetics; 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; Physiological aspects; Prokaryotic Initiation Factor-2; Protein binding; Protein Biosynthesis; Protein Conformation; Protein Structure, Secondary; Protein synthesis; Proteins; Ribonucleic acid; Ribosomes - metabolism; RNA; RNA, Transfer, Amino Acyl - chemistry; RNA, Transfer, Amino Acyl - metabolism; Scientific Concepts; Structure in molecular biology; Synthesis; Thermus; Thermus aquaticus; Translation; Translation. Translation factors. Protein processing; Yeast
• ISSN: 0036-8075; 1095-9203
• 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.