Protein biosynthesis: structural studies of the elongation cycle

FEBS Letters

Nyborg, Jens²  Liljas, Anders¹ 

[1] Department of Molecular Biophysics, Center for Chemistry and Chemical Engineering, University of Lund, P.O. Box 124, S-221 00 Lund, Sweden;Department of Molecular and Structural Biology, University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark

关键词: Protein synthesis;    Structural analysis;    Elongation factor;    Crystallography;    Electron cryomicroscopy;   

DOI  :  10.1016/S0014-5793(98)00624-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The elongation cycle of protein synthesis on ribosomes is catalyzed by the elongation factors EF-Tu and EF-G. A thorough crystallographic analysis of the structures of the different functional states of EF-Tu has been made. Furthermore, the structure of EF-G:GDP is the form of EF-G that dissociates from the ribosome. Since it mimics the structure of the ternary complex of EF-Tu:GTP with aminoacyl-tRNA, which subsequently binds to the ribosome, EF-G:GDP leaves an imprint on the ribosome for the ternary complex. In addition, electron cryomicroscopy studies of ribosomes with tRNA as well as the ternary complex bound are beginning to give a solid structural basis for the functional description of elongation.

【 授权许可】

Unknown