Structural basis of signal-sequence recognition by the signal recognition particle
Structural basis of signal-sequence recognition by the signal recognition particle
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DOI：
10.1038/nsmb.1994
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发表时间：
2011-03-01
影响因子：
16.8
通讯作者：
Sauer-Eriksson, A. Elisabeth
中科院分区：
文献类型：
--
作者：
Hainzl, Tobias;Huang, Shenghua;Sauer-Eriksson, A. Elisabeth
信号识别颗粒（SRP）识别并结合新生蛋白质从核糖体中出现的信号序列。我们在这里提出的3.0埃结构的信号序列绑定到詹氏甲烷球菌SRP核心。与游离SRP核心的结构比较表明，信号序列结合诱导GM-接头螺旋的形成和NG结构域结构变化的180度翻转，这确保了蛋白质靶向过程中事件的分层连续。
The signal recognition particle (SRP) recognizes and binds the signal sequence of nascent proteins as they emerge from the ribosome. We present here the 3.0-angstrom structure of a signal sequence bound to the Methanococcus jannaschii SRP core. Structural comparison with the free SRP core shows that signal-sequence binding induces formation of the GM-linker helix and a 180 degrees flip of the NG domain-structural changes that ensure a hierarchical succession of events during protein targeting.