Structural information for explaining the molecular mechanism of protein biosynthesis

FEBS Letters

Nyborg, Jens¹  Clark, Brian F.C¹  Kjeldgaard, Morten¹  Thirup, Søren¹ 

[1] Institute of Molecular and Structural Biology, University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Aarhus, Denmark

关键词: Protein biosynthesis;    RNA world;    Macromolecular mimicry;    Protein evolution;    Elongation factor;    Translation factor;    Structure determination;    Crystallography;    Electron cryo-microscopy;   

DOI  :  10.1016/S0014-5793(99)00562-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Protein biosynthesis is controlled by a number of proteins external to the ribosome. Of these, extensive structural investigations have been performed on elongation factor-Tu and elongation factor-G. This now gives a rather complete structural picture of the functional cycle of elongation factor-Tu and especially of the elongation phase of protein biosynthesis. The discovery that three domains of elongation factor-G are structurally mimicking the amino-acylated tRNA in the ternary complex of elongation factor-Tu has been the basis of much discussion of the functional similarities and functional differences of elongation factor-Tu and elongation factor-G in their interactions with the ribosome. Elongation factor-G:GDP is now thought to leave the ribosome in a state ready for checking the codon-anticodon interaction of the aminoacyl-tRNA contained in the ternary complex of elongation factor-Tu. Elongation factor-G does this by mimicking the shape of the ternary complex. Other translation factors such as the initiation factor-2 and the release factor 1 or 2 are also thought to mimic tRNA. These observations raise questions concerning the possible evolution of G-proteins involved in protein biosynthesis.

【 授权许可】

Unknown