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Science 1 December 1995:
Vol. 270. no. 5241, pp. 1464 - 1472
DOI: 10.1126/science.270.5241.1464
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Research Articles

Crystal Structure of the Ternary Complex of Phe-tRNA, EF-Tu, and a GTP Analog

Poul Nissen,  Morten Kjeldgaard,  Søren Thirup,  Galina Polekhina,  Ludmila Reshetnikova,  Brian F. C. Clark,  Jens Nyborg (1)

The structure of the ternary complex consisting of yeast phenylalanyl-transfer RNA (Phe-tRNA), 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-tRNA 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.


P. Nissen, M. Kjeldgaard, S. Thirup, G. Polekhina, B. F. C. Clark, and J. Nyborg are in the Department of Biostructural Chemistry, Institute of Chemistry, Aarhus University, Langelandsgade 140, DK-8000 Aarhus C, Denmark. L. Reshetnikova is at the Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 32 Vavilov str., 117984 Moscow, Russia.
(1) To whom correspondence should be addressed.


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Translation Elongation Factor 1 Functions in the Yeast Saccharomyces cerevisiae.
M. ANAND, L. VALENTE, A. CARR-SCHMID, R. MUNSHI, O. OLAREWAJU, P.A. ORTIZ, and T.G. KINZY (2001)
Cold Spring Harb Symp Quant Biol 66, 439-448
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Protein tRNA Mimicry in Translation Termination.
Y. NAKAMURA, M. UNO, T. TOYODA, T. FUJIWARA, and K. ITO (2001)
Cold Spring Harb Symp Quant Biol 66, 469-476
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The Ribosome in the 21st Century: The Post-structural Era.
P.B. MOORE (2001)
Cold Spring Harb Symp Quant Biol 66, 607-614
   Abstract »    PDF »
Evidence for Horizontal Gene Transfer in Evolution of Elongation Factor Tu in Enterococci.
D. Ke, M. Boissinot, A. Huletsky, F. J. Picard, J. Frenette, M. Ouellette, P. H. Roy, and M. G. Bergeron (2000)
J. Bacteriol. 182, 6913-6920
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Physical and Functional Interaction between the Eukaryotic Orthologs of Prokaryotic Translation Initiation Factors IF1 and IF2.
S. K. Choi, D. S. Olsen, A. Roll-Mecak, A. Martung, K. L. Remo, S. K. Burley, A. G. Hinnebusch, and T. E. Dever (2000)
Mol. Cell. Biol. 20, 7183-7191
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The C-terminal Subdomain (IF2 C-2) Contains the Entire fMet-tRNA Binding Site of Initiation Factor IF2.
R. Spurio, L. Brandi, E. Caserta, C. L. Pon, C. O. Gualerzi, R. Misselwitz, C. Krafft, K. Welfle, and H. Welfle (2000)
J. Biol. Chem. 275, 2447-2454
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Crystal Structure of Thermotoga maritima Ribosome Recycling Factor: A tRNA Mimic.
M. Selmer, S. Al-Karadaghi, G. Hirokawa, A. Kaji, and A. Liljas (1999)
Science 286, 2349-2352
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Quality Control Mechanisms During Translation.
M. Ibba and a. D. Söll (1999)
Science 286, 1893-1897
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