Molecular Mimicry in Protein Synthesis?
- 1 December 1995
- journal article
- editorial
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 270 (5241) , 1453
- https://doi.org/10.1126/science.270.5241.1453
Abstract
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.This publication has 9 references indexed in Scilit:
- Crystal Structure of the Ternary Complex of Phe-tRNA Phe , EF-Tu, and a GTP AnalogScience, 1995
- Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus.The EMBO Journal, 1994
- The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformationStructure, 1993
- Crystal structure of active elongation factor Tu reveals major domain rearrangementsNature, 1993
- Refined structure of elongation factor EF-Tu from Escherichia coliJournal of Molecular Biology, 1992
- RIBOSOMAL RNA AND TRANSLATIONAnnual Review of Biochemistry, 1991
- Ribosomal Translocation: Facts and ModelsProgress in Nucleic Acid Research and Molecular Biology, 1985
- The role of guanosine 5′-triphosphate in polypeptide chain elongationBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1978