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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structural basis for the attachment of a paramyxoviral polymerase to its template.
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Structural basis for the attachment of a paramyxoviral polymerase to its template.

机译：副粘病毒聚合酶与其模板结合的结构基础。

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摘要

The nucleocapsid of measles virus is the template for viral RNA synthesis and is generated through packaging of the genomic RNA by the nucleocapsid protein (N). The viral polymerase associates with the nucleocapsid through a small, trihelical binding domain at the carboxyl terminus of the phosphoprotein (P). Translocation of the polymerase along the nucleocapsid during RNA synthesis is thought to involve the repeated attachment and release of the binding domain. We have investigated the interaction between the binding domain from measles P (amino acids 457-507) and the sequence it recognizes within measles N (amino acids 477-505). By using both solution NMR spectroscopy and x-ray crystallography, we show that N(487-503) binds as a helix to the surface created by the second (alpha2) and third (alpha3) helices of P(457-507), in an orientation parallel to the helix alpha3, creating a four-helix bundle. The binding interface is tightly packed and dominated by hydrophobic amino acids. Binding and folding ofN(487-503) are coupled. However, when not bound to P, N(487-503) does not resemble a statistical random coil but instead exists in a loosely structured state that mimics the bound conformation. We propose that before diffusional encounter, the ensemble of accessible conformations for N(487-503) is biased toward structures capable of binding P, facilitating rapid association of the two proteins. This study provides a structural analysis of polymerase-template interactions in a paramyxovirus and presents an example of a protein-protein interaction that must be only transiently maintained as part of its normal function.
机译：麻疹病毒的核衣壳是病毒RNA合成的模板，是通过核衣壳蛋白（N）包装基因组RNA产生的。病毒聚合酶通过磷蛋白（P）羧基末端的三螺旋小结合域与核衣壳结合。在RNA合成过程中，聚合酶沿核衣壳的移位被认为涉及结合域的重复附着和释放。我们已经研究了来自麻疹P（氨基酸457-507）的结合域与它在麻疹N（氨基酸477-505）中识别的序列之间的相互作用。通过使用溶液NMR光谱学和X射线晶体学，我们显示N（487-503）作为螺旋结合到P（457-507）的第二（alpha2）和第三（alpha3）螺旋产生的表面上，平行于螺旋alpha3的方向，创建了一个四螺旋束。结合界面紧密堆积，并以疏水氨基酸为主。 N（487-503）的绑定和折叠是耦合的。但是，当不绑定到P时，N（487-503）并不类似于统计随机线圈，而是以模仿绑定构象的松散结构状态存在。我们建议在扩散相遇之前，N（487-503）的可及构象的集合偏向于能够结合P的结构，从而促进两种蛋白质的快速缔合。这项研究提供了副粘病毒中聚合酶-模板相互作用的结构分析，并提供了一个蛋白质-蛋白质相互作用的例子，该蛋白质-蛋白质相互作用只能作为其正常功能的一部分而暂时维持。

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