Structure of the ternary complex of EF-Tu: macromolecular mimicry in translation

• Published in: Trends in biochemical sciences (Amsterdam. Regular ed.) 1996-03, Vol.21 (3), p.81-82
• Main Authors: Nyborg, J, Nissen, P, Kjeldgaard, M, Thirup, S, Polekhina, G, Clark, B F
• Format: Article
• Language: English
• Subjects: Binding Sites; GTP-Binding Proteins - metabolism; Guanosine Diphosphate - metabolism; Guanosine Triphosphate - analogs & derivatives; Guanosine Triphosphate - chemistry; Guanosine Triphosphate - metabolism; Macromolecular Substances; Models, Molecular; Molecular Mimicry; Peptide Elongation Factor Tu - chemistry; Peptide Elongation Factor Tu - metabolism; Protein Biosynthesis; Protein Structure, Secondary; RNA, Transfer, Phe - chemistry; RNA, Transfer, Phe - metabolism; Thermus aquaticus
• ISSN: 0968-0004
• DOI: 10.1016/0968-0004(96)30008-X

Protein biosynthesis is a well described process, the basic features of which are found in many biochemistry text books. However, detailed structural information about important aspects of the process have been lacking for some time. Most information has been available on aminoacyl-tRNA synthetases. Here, we will concentrate on the newly obtained structural information on the ternary complex of Phe-tRNA, elongation factor Tu (EF-Tu) and the GTP analogue GDPNP. The implications of this structure for its interaction with the ribosome will be discussed. The structural significance of the ternary complex regarding protein synthesis and a comparison with elongation factor G (EF-G) will also be discussed. The observed macromolecular mimicry between the ternary complex and EF-G allows the formulation of a common new concept for all G proteins involved in protein biosynthesis.