title: Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog.
abstract: 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.
mesh_terms: D000595:Amino Acid Sequence; D000926:Anticodon; D001483:Base Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D006153:Guanosine Diphosphate / Q000737:chemistry / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D006639:Histidine / Q000378:metabolism; D008239:Lysine / Q000378:metabolism; D008958:Models, Molecular; D018716:Molecular Mimicry; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D020653:Peptide Elongation Factor G; D010444:Peptide Elongation Factor Tu / Q000737:chemistry* / Q000378:metabolism; D010445:Peptide Elongation Factors / Q000737:chemistry / Q000378:metabolism; D010448:Peptide Initiation Factors / Q000737:chemistry / Q000378:metabolism; D010454:Peptide Termination Factors / Q000737:chemistry / Q000378:metabolism; D039881:Prokaryotic Initiation Factor-2; D014176:Protein Biosynthesis; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012346:RNA, Transfer, Amino Acyl / Q000737:chemistry* / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism; D013824:Thermus
chemical_list: D000926:Anticodon; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors; D010448:Peptide Initiation Factors; D010454:Peptide Termination Factors; D039881:Prokaryotic Initiation Factor-2; D012346:RNA, Transfer, Amino Acyl; D006153:Guanosine Diphosphate; D006639:Histidine; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu; D008239:Lysine