共 48 条
Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation
被引:251
作者:

Stark, H
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机构: Univ Witten Herdecke, Inst Mol Biol, D-58448 Witten, Germany

Rodnina, MV
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h-index: 0
机构: Univ Witten Herdecke, Inst Mol Biol, D-58448 Witten, Germany

Wieden, HJ
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h-index: 0
机构: Univ Witten Herdecke, Inst Mol Biol, D-58448 Witten, Germany

van Heel, M
论文数: 0 引用数: 0
h-index: 0
机构: Univ Witten Herdecke, Inst Mol Biol, D-58448 Witten, Germany

Wintermeyer, W
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机构:
Univ Witten Herdecke, Inst Mol Biol, D-58448 Witten, Germany Univ Witten Herdecke, Inst Mol Biol, D-58448 Witten, Germany
机构:
[1] Univ Witten Herdecke, Inst Mol Biol, D-58448 Witten, Germany
[2] Univ London Imperial Coll Sci Technol & Med, Dept Biochem, London SW7 2AY, England
来源:
关键词:
D O I:
10.1016/S0092-8674(00)80666-2
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:
Elongation factor (EF) G promotes tRNA translocation on the ribosome. We present three-dimensional reconstructions, obtained by cryo-electron microscopy, of EF-G-ribosome complexes before and after translocation. In the pretranslocation state, domain 1 of EF-G interacts with the L7/12 stalk on the 50S subunit, while domain 4 contacts the shoulder of the 30S subunit in the region where protein S4 is located. During translocation, EF-G experiences an extensive reorientation, such that, after translocation, domain 4 reaches into the decoding center. The factor assumes different conformations before and after translocation. The structure of the ribosome is changed substantially in the pretranslocation state, in particular at the head-to-body junction in the 30S subunit, suggesting a possible mechanism of translocation.
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页码:301 / 309
页数:9
相关论文
共 48 条
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