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The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation

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  • Bioinformatics Research Centre (BiRC)
  • Interdisciplinary Nanoscience Center
  • Department of Molecular Biology
  • Department of Molecular Biology
BACKGROUND: Elongation factor Tu (EF-Tu) is a GTP-binding protein that is crucial for protein biosynthesis. In the GTP form of the molecule, EF-Tu binds tightly to aminoacyl-tRNA, forming a ternary complex that interacts with the ribosomal acceptor site. During this interaction, GTP is hydrolyzed, and EF-Tu.GDP is ejected. RESULTS: The crystal structure of EF-Tu from Thermus aquaticus, complexed to the GTP analogue GDPNP, has been determined at 2.5 A resolution and compared to the structure of Escherichia coli EF-Tu.GDP. During the transition from the GDP (inactive) to the GTP (active) form, domain 1, containing the GTP-binding site, undergoes internal conformational changes similar to those observed in ras-p21. In addition, a dramatic rearrangement of domains is observed, corresponding to a rotation of 90.8 degrees of domain 1 relative to domains 2 and 3. Residues that are affected in the binding of aminoacyl-tRNA are found in or near the cleft formed by the domain interface. CONCLUSION: GTP binding by EF-Tu leads to dramatic conformational changes which expose the tRNA binding site. It appears that tRNA binding to EF-Tu induces a further conformational change, which may affect the GTPase activity.
Original languageEnglish
JournalStructure
Volume1
Issue1
Pages (from-to)35-50
Number of pages15
ISSN0969-2126
Publication statusPublished - 1993

    Research areas

  • Amino Acid Sequence, Crystallography, X-Ray, Escherichia coli, Guanosine Triphosphate, Models, Molecular, Molecular Sequence Data, Peptide Elongation Factor Tu, Protein Structure, Secondary, Sequence Homology, Amino Acid, Software, Thermus

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