EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome
EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome
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DOI：
10.1038/10695
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发表时间：
1999-07-01
期刊：
影响因子：
--
通讯作者：
Frank, J
中科院分区：
文献类型：
--
作者：
Agrawal, RK;Heagle, AB;Frank, J
低温电镜观察了GDP和GTP状态下70S核糖体上的延伸因子G （EF-G）。GTP水解是EF-G所有结构域与易位前复合物结合和完成易位所必需的，此外，在核糖体中发现了大的构象变化，30S亚基的头部向L1蛋白一侧移动，并且在EF-G结合后L7/L12柄分叉。在GTP水解后，分叉被逆转，在茎的基部和EF-G之间形成了一种类似于棒状的连接。
Cryo-electron microscopy has been used to visualize elongation factor G (EF-G) on the 70S ribosome in GDP and GTP states. GTP hydrolysis is required for binding of all the domains of EF-G to the pretranslocational complex and for the completion of translocation, in addition, large conformational changes have been identified in the ribosome, The head of the 30S subunit shifts toward the L1 protein side, and the L7/L12 stalk becomes bifurcated upon EF-G binding. Upon GTP hydrolysis, the bifurcation is reversed and an are-like connection is formed between the base of the stalk and EF-G.