Signal-sequence induced conformational changes in the signal recognition particle.
Signal-sequence induced conformational changes in the signal recognition particle.
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DOI：
10.1038/ncomms8163
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发表时间：
2015-06-08
影响因子：
16.6
通讯作者：
Sauer-Eriksson, A. Elisabeth
中科院分区：
文献类型：
--
作者：
Hainzl, Tobias;Sauer-Eriksson, A. Elisabeth
共翻译蛋白质靶向是将新生蛋白质递送至适当细胞膜的必需的、进化上保守的途径。在该途径中，信号识别颗粒（SRP）首先识别新生蛋白的N-末端信号序列，随后与SRP受体相互作用。为此，结合在SRP 54 M结构域中的信号序列必须有效地传递到与受体相互作用的SRP 54 NG结构域。在这里，我们提出了2.9纳米晶体结构的未结合和信号序列结合的SRP形式，都存在于不对称单位。这些结构为偶联结合和折叠机制提供了证据，其中信号序列结合诱导GM接头螺旋、指状环和C末端α螺旋αM6的协同折叠。这种机制允许结合位点的高度结构适应性，并表明M结构域中的信号序列结合如何与NG结构域的重新定位相耦合。 信号识别颗粒在膜蛋白和分泌蛋白的共翻译蛋白靶向中起着关键作用。在这里，作者报告了信号序列结合和未结合形式的三元SRP复合物的晶体结构，提供了信号序列结合如何与SRP受体相互作用耦合的见解。
Co-translational protein targeting is an essential, evolutionarily conserved pathway for delivering nascent proteins to the proper cellular membrane. In this pathway, the signal recognition particle (SRP) first recognizes the N-terminal signal sequence of nascent proteins and subsequently interacts with the SRP receptor. For this, signal sequence binding in the SRP54 M domain must be effectively communicated to the SRP54 NG domain that interacts with the receptor. Here we present the 2.9 Å crystal structure of unbound- and signal sequence bound SRP forms, both present in the asymmetric unit. The structures provide evidence for a coupled binding and folding mechanism in which signal sequence binding induces the concerted folding of the GM linker helix, the finger loop, and the C-terminal alpha helix αM6. This mechanism allows for a high degree of structural adaptability of the binding site and suggests how signal sequence binding in the M domain is coupled to repositioning of the NG domain. The signal recognition particle plays a key role in the co-translational protein targeting of membrane and secretory proteins. Here the authors report a crystal structure of the ternary SRP complex in signal sequence bound and unbound forms, providing insight into how signal sequence binding is coupled to SRP receptor interaction.
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DOI：
10.1126/science.1165971
发表时间：
2009-01-02
期刊：
Science (New York, N.Y.)
影响因子：
--
作者：
Bradshaw N;Neher SB;Booth DS;Walter P
通讯作者：
Walter P
DOI：
10.1073/pnas.2436132100
发表时间：
2003-12-09
影响因子：
11.1
作者：
Rosendal, KR;Wild, K;Sinning, L
通讯作者：
Sinning, L
影响因子：
16.8
作者：
Hainzl, Tobias;Huang, Shenghua;Sauer-Eriksson, A. Elisabeth
通讯作者：
Sauer-Eriksson, A. Elisabeth
影响因子：
4.8
作者：
Noriega, Thomas R.;Tsai, Albert;Walter, Peter
通讯作者：
Walter, Peter
DOI：
10.1107/s0907444909052925
发表时间：
2010-02
期刊：
Acta crystallographica. Section D, Biological crystallography
影响因子：
--
作者：
Adams PD;Afonine PV;Bunkóczi G;Chen VB;Davis IW;Echols N;Headd JJ;Hung LW;Kapral GJ;Grosse-Kunstleve RW;McCoy AJ;Moriarty NW;Oeffner R;Read RJ;Richardson DC;Richardson JS;Terwilliger TC;Zwart PH
通讯作者：
Zwart PH