Structural dissection of human metapneumovirus phosphoprotein using small angle x-ray scattering.

Structural dissection of human metapneumovirus phosphoprotein using small angle x-ray scattering.
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DOI:
10.1038/s41598-017-14448-z
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发表时间:
2017-11-01
期刊:
影响因子:
4.6
通讯作者:
Leyrat C
Leyrat C
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Renner M;Paesen GC;Grison CM;Granier S;Grimes JM;Leyrat C

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磷酸蛋白(P)是非分段、负链RNA病毒RNA聚合酶(L)的主要和必需的辅助因子。P将病毒聚合酶定位到其核蛋白- rna模板上,并作为核蛋白(N)的伴侣,从而防止细胞rna的非特异性封装。人偏肺病毒(HMPV)的磷蛋白形成由稳定的寡聚结构域(Pcore)和大的内在无序区(IDRs)组成的同型四聚体。在这里,我们将Pcore的x射线晶体学与基于小角x射线散射(SAXS)的全长P蛋白及其几个片段的集合建模相结合,提供了P的结构描述,捕捉了其动态特征,并突出了idr中不同稳定结构元素的存在。我们讨论了HMPV P的结构特性对病毒转录/复制机制的组装和功能的影响。
The phosphoprotein (P) is the main and essential cofactor of the RNA polymerase (L) of non-segmented, negative‐strand RNA viruses. P positions the viral polymerase onto its nucleoprotein–RNA template and acts as a chaperone of the nucleoprotein (N), thereby preventing nonspecific encapsidation of cellular RNAs. The phosphoprotein of human metapneumovirus (HMPV) forms homotetramers composed of a stable oligomerization domain (Pcore) flanked by large intrinsically disordered regions (IDRs). Here we combined x-ray crystallography of Pcore with small angle x-ray scattering (SAXS)-based ensemble modeling of the full-length P protein and several of its fragments to provide a structural description of P that captures its dynamic character, and highlights the presence of varyingly stable structural elements within the IDRs. We discuss the implications of the structural properties of HMPV P for the assembly and functioning of the viral transcription/replication machinery.
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