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Science 1 December 1995:
Vol. 270. no. 5241, p. 1453
DOI: 10.1126/science.270.5241.1453
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Perspectives

Peter B. Moore

A Research Article in this issue of Science by P. Nissen et al. (p. 1464) reports the crystal structure of elongation factor Tu (EF-Tu) complexed with tRNA and GTP. In his Perspective, P. Moore discusses the similarity between this new structure and the GDP-bound form of elongation factor G. Three domains at the carboxyl-terminal end of EF-G, which have no homologs in EF-Tu, together resemble tRNA and are positioned like the tRNA bound to EF-Tu.

The author is in the Departments of Chemistry and Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 05620-8107, USA. E-mail: moore@proton.chem.yale.edu

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
BPOZ-2 directly binds to eEF1A1 to promote eEF1A1 ubiquitylation and degradation and prevent translation..
K. Koiwai, S. Maezawa, T. Hayano, M. Iitsuka, and O. Koiwai (2008)
Genes Cells 13, 593-607
   Abstract »    Full Text »    PDF »
Ratchet-like Movements between the Two Ribosomal Subunits: Their Implications in Elongation Factor Recognition and tRNA Translocation.
J. FRANK and R.K. AGRAWAL (2001)
Cold Spring Harb Symp Quant Biol 66, 67-76
   Abstract »    PDF »
Complex Formation of the Elongation Factor Tu from Pseudomonas aeruginosa with Nucleoside Diphosphate Kinase Modulates Ribosomal GTP Synthesis and Peptide Chain Elongation.
S. Mukhopadhyay, S. Shankar, W. Walden, and A. M. Chakrabarty (1997)
J. Biol. Chem. 272, 17815-17820
   Abstract »    Full Text »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)