New Structural Data on Elongation Factor-Tu:Gdp Based on X-Ray Crystallography

  • J. Nyborg
  • T. la Cour


The GDP binding proteins (G-proteins) have attracted much attention in recent years for many good reasons. One good reason is that some of these represent a biomolecular switching mechanism with a possibility of amplification of extracellular signals. Most (if not all) have a specific GDP- binding domain of about 200 residues. This domain can be in an “on-state” complexed with GTP. This state is transformed to the “off-state” by hydrolysis of GTP to GDP. The G-proteins in their “on-state” influence the reactions of other proteins to amplify the signal.


Secondary Structure Element Phosphoryl Group Ternary Complex Formation Guanosine Diphosphate Topology Diagram 
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  1. B. Antonsson and R. Leberman (1984) “Modification of Amino Groups in EF-Tu.GTP and the Terrnary Complex EF-Tu.GTP. Valyl-tRNAVal”, Eur. J. Biochem., 141, 483–487.PubMedCrossRefGoogle Scholar
  2. U.W. Arndt and A.J. Wonacott, Eds. (1977) “The Rotation Method in Crystallography”, North-Holland Publishing Company, AmsterdamGoogle Scholar
  3. T.L. Blundell and L. N. Johnson (1976) “Protein Crystallography”, Academic Press, London.Google Scholar
  4. C.-I. Brändén (1980) “Relation between structure and function of a/ß-proteins”. Qt. Rev. Biophys., 13, 317–338.CrossRefGoogle Scholar
  5. Y. Cenatiempo, F. Deville, J. Dondon, M. Grunberg-Manago, C. Sacerdot, J.W.B. Hershey, H.F. Hansen, H.U. Petersen, B.F.C. Clark, M. Kjeldgaard, T.F.M. la Cour, K.K. Mortensen and J. Nyborg (1987) “The Protein Synthesis Initiation Factor 2 G-Domain. Study of a Functionally Active C-Terminal 65-Kilodalton Fragment of IF2 from Escherichia coli”, Biochem., 26, 5070–5076.CrossRefGoogle Scholar
  6. T.F.M. la Cour, J. Nyborg, S. Thirup and B.F.C. Clark (1985) “Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography”, EMBO J., 4, 2385–2388.PubMedGoogle Scholar
  7. T.E. Dever, M.J. Glymias and W.C. Merrick (1987) “The GTP-Binding Domain: Three Consensus sequence Elements with Distinct Spacing”, P.N.A.S., 84, 1814–1818.PubMedCrossRefGoogle Scholar
  8. F.J. Duisterwinkel, B. Kraal, J.M. de Graaf, A. Talens, L. Bosch, G.W.M. Swart, A. Parmeggiani, T.F.M. la Cour, J. Nyborg and B.F.C. Clark (1984) “Specific alterations of the EF-Tu polypeptide chain considered in the light of its three-dimensional structure”, EMBO J., 3, 113–120.PubMedGoogle Scholar
  9. K.R. Halliday (1984) “Regional Homology in GTP-binding Proto-Oncogone Products and Elongation Factors”, J. Cycl. Nucl. Prot. Phos. Res., 9, 435–448.Google Scholar
  10. F. Hanic, O. Lindquist, J. Nyborg and A. Zedier (1971) “The Crystal Structure of MgO. 3B2O3.5H2O)”, Coll. Czech. Chem. Comm., 36, 3678–3701.CrossRefGoogle Scholar
  11. W.G.J. Hol, P.T. van Duijnen and H.J.C. Berendsen (1978) “The a-helix dipole and the properties of proteins”, Nature, 273, 443–446.PubMedCrossRefGoogle Scholar
  12. J. Jonak, T.E. Petersen, B. Meloun and I. Rychlik (1984) “Histidine residues in elongation factor EF-Tu from Escherichia coli protected by aminoacyl-tRNA against photo-oxidation” Eur. J. Biochem., 144, 295–303.PubMedCrossRefGoogle Scholar
  13. F. Jurnak (1985) “Structure of the GDP Domain of EF-Tu and Location of the Amino Acids Homologous to ras Oncogene Proteins”, Science, 230, 32–36.PubMedCrossRefGoogle Scholar
  14. F. Jurnak (1988) “The three-dimensional structure of c-H-ras p21: Implications for oncogene and G protein studies”, TIBS, 13, 195–198.PubMedGoogle Scholar
  15. R. Leberman and U. Egner (1984) “Homologies in the primary structure of GTP-binding proteins: the nucleotide-binding site of EF-Tu and p21”, EMBO J., 3, 339–341.PubMedGoogle Scholar
  16. M. Levitt and C. Chotia (1976), “Structural Patterns in Globular Proteins”, Nature, 261, 552–557.PubMedCrossRefGoogle Scholar
  17. F. McCormick, B.F.C. Clark, T. F. M. la Cour, M. Kjeldgaard, L. Norskov-Lauritsen and J. Nyborg (1985), “A Model for the Tertiary structure of p21, the Product of the ras Oncogene”, Science, 230, 78–82.PubMedCrossRefGoogle Scholar
  18. D.L. Miller and H. Weissbach (1977), “The interactions of Elongation Factor Tu”, in “Nucleic Acid-Protein Recognition”, 409–440, Academic Press, New York.CrossRefGoogle Scholar
  19. K. Morikawa, T.F.M. la Cour, J. Nyborg, K.M. Rasmussen, D. L. Miller and B. F. C. Clark (1978), “High Resolution X-ray Crystallographic Analysis of a Modified Form of the Elongation Factor Tu: Guanosine Disphosphate Complex”, J. Mol. Biol., 125, 325–338.PubMedCrossRefGoogle Scholar
  20. W. Möller and R. Amons (1985) “Phosphate-binding sequences in nucleotide-binding proteins”, FEBS Lett., 186, 1–7.PubMedCrossRefGoogle Scholar
  21. J.M. van Noort, B. Kraal, L. Bosch, T.F.M. la Cour, J. Nyborg and B.F.C. Clark (1984) “Crosslinking of tRNA at two diffrent sites of the elongation factor Tu”, P.N.A.S. 81, 3969–3972.PubMedCrossRefGoogle Scholar
  22. J. Nyborg and J. Danielsen (1970), “Direct Determination of the Crystal Structure of Bis (dichlorophosphate) bis (phosphorylchloride) Magnesium: Mg (PO2Cl2)2 (POCl3)2”, Acta Chem. Scand., 24, 59–71.CrossRefGoogle Scholar
  23. M.P. Prinz and D.L. Miller (1973) “Evidence for Conformational Changes in Elongation Factor Tu Induced by GTP and GDP”, Biochem. Biophys. Res. Commun., 53, 149–156.CrossRefGoogle Scholar
  24. J.S. Richardson (1981), “The Anatomy and Taxonomy of Protein Structure”, Adv. Protein. Chem., 34, 167–339.PubMedCrossRefGoogle Scholar
  25. G.E. Schulz and R.H. Schirmer (1979), “Principles of Protein Structure”, Springer-Verlag, Heidelberg.CrossRefGoogle Scholar
  26. M. Sprinzl (1987) “Affinity labelling of the GDP/GTP binding site in Thermus thermophilus Elongation Factor Tu”, Personal communication.Google Scholar
  27. D. Suck and W. Kabsch (1981), “X-ray Determination of the GDP-binding site of Escherihia coli Elongation Factor Tu by Substitution with ppGpp”, FEBS Lett., 126, 120–122.PubMedCrossRefGoogle Scholar
  28. A. M. de Vos, L. Tong, M. V. Milburn, P.M. Matias, J. Jancarik, S. Noguchi, S. Nishimura, K. Miura, E. Ohtsuka and S.-H. Kim (1988) “Three-Dimensional Structure of an Oncogene Protein: Catalytic Domain of Human c-H-ras p21”, Science, 239, 888–893.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1989

Authors and Affiliations

  • J. Nyborg
    • 1
  • T. la Cour
    • 1
  1. 1.Department of Biostructural ChemistryUniversity of AarhusAarhus CDenmark

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