Protein biosynthesis: structural studies of the elongation cycle

被引:21
作者
Nyborg, J
Liljas, A
机构
[1] Aarhus Univ, Dept Mol & Struct Biol, DK-8000 Aarhus C, Denmark
[2] Lund Univ, Dept Mol Biophys, Ctr Chem & Chem Engn, S-22100 Lund, Sweden
来源
FEBS LETTERS | 1998年 / 430卷 / 1-2期
关键词
protein synthesis; structural analysis; elongation factor; crystallography; electron cryomicroscopy;
D O I
10.1016/S0014-5793(98)00624-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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:CTP 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. (C) 1998 Federation of European Biochemical Societies.
引用
收藏
页码:95 / 99
页数:5
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