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Macromolecular mimicry in protein biosynthesis

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  • Bioinformatics Research Centre (BiRC)
  • Interdisciplinary Nanoscience Center
  • Department of Molecular Biology
  • Department of Molecular Biology
Elongation factor Tu (EF-Tu) is a G-protein which, in its active GTP conformation, protects and carries aminoacylated tRNAs (aa-tRNAs) to the ribosome during protein biosynthesis. EF-Tu consists of three structural domains of which the N-terminal domain consists of two special regions (switch I and switch II) which are structurally dependent on the type of the bound nucleotide. Structural studies of the complete functional cycle of EF-Tu reveal that it undergoes rather spectacular conformational changes when activated from the EF-Tu.GDP form to the EF-Tu.GTP form. In its active form, EF-Tu.GTP without much further structural change interacts with aa-tRNAs in the so-called ternary complex. The conformational changes of EF-Tu involve rearrangements of the secondary structures of both the switch I and switch II regions. As the switch II region forms part of the interface between domains 1 and 3, its structural rearrangement results in a very large change of the position of domain 1 relative to domains 2 and 3. The overall shape of the ternary complex is surprisingly similar to the overall shape of elongation factor G (EF-G). Thus, three domains of the protein EF-G seem to mimic the tRNA part of the ternary complex. This macromolecular mimicry has profound implications for the function of the elongation factors on the ribosome.
Original languageEnglish
JournalStructure
Volume2
Issue3
Pages (from-to)S7-11
ISSN0969-2126
Publication statusPublished - 1997

    Research areas

  • Amino Acid Sequence, Guanosine Diphosphate, Guanosine Triphosphate, Macromolecular Substances, Models, Molecular, Molecular Mimicry, Molecular Sequence Data, Peptide Chain Elongation, Translational, Peptide Elongation Factor Tu, Protein Biosynthesis, Protein Folding, Protein Structure, Secondary, Sequence Homology, Amino Acid

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