Intrinsic dynamics of the partly unstructured PX domain from the Sendai virus RNA polymerase cofactor P.
Intrinsic dynamics of the partly unstructured PX domain from the Sendai virus RNA polymerase cofactor P.
复制标题
仙台病毒 RNA 聚合酶辅因子 P 部分非结构化 PX 结构域的内在动力学。
作者：
Klaartje Houben;L. Blanchard;M. Blackledge;D. Marion
尽管它们对功能的重要性显而易见，但对本质上非结构化蛋白质的动力学知之甚少。仙台病毒磷蛋白是RNA聚合酶的辅因子，含有部分非结构化的蛋白质结构域。磷蛋白X结构域（PX）负责将聚合酶结合到组装病毒RNA的核衣壳上。对于RNA合成，非结构化和结构化PX亚结构域的动力学相互作用被认为驱动RNA聚合酶沿着核衣壳前进。在这里，我们提出了一个详细的研究PX使用氢/氘交换和不同的NMR弛豫测量的动力学。在非结构化的子域，大幅度快速运动被发现微调的存在下与短侧链的残留物。在结构化的子域中，其中主链和侧链的快速运动受到相当的限制，第一螺旋经历对应于局部展开事件的缓慢构象交换。其他两个螺旋，这代表的核衣壳结合位点，被认为是更稳定的，并重新定向相对于彼此，探测由缓慢的构象交换确定的残基上的第三个螺旋。该研究阐明了这种部分非结构化蛋白质的内在微分动力学，并提出了这些动力学与其功能之间的关系。
Despite their evident importance for function, dynamics of intrinsically unstructured proteins are poorly understood. Sendai virus phosphoprotein, cofactor of the RNA polymerase, contains a partly unstructured protein domain. The phosphoprotein X domain (PX) is responsible for binding the polymerase to the nucleocapsid assembling the viral RNA. For RNA synthesis, the interplay of the dynamics of the unstructured and structured PX subdomains is thought to drive progression of the RNA polymerase along the nucleocapsid. Here we present a detailed study of the dynamics of PX using hydrogen/deuterium exchange and different NMR relaxation measurements. In the unstructured subdomain, large amplitude fast motions were found to be fine-tuned by the presence of residues with short side chains. In the structured subdomain, where fast motions of both backbone and side chains are fairly restricted, the first helix undergoes slow conformational exchange corresponding to a local unfolding event. The other two helices, which represent the nucleocapsid binding site, were found to be more stable and to reorient with respect to each other, as probed by slow conformational exchange identified for residues on the third helix. The study illustrates the intrinsically differential dynamics of this partly unstructured protein and proposes the relation between these dynamics and its function.
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影响因子：
3.7
作者：
S. Horikami;S. Moyer
通讯作者：
S. Horikami;S. Moyer
无模型公式的检验。
DOI：
10.1006/jmrb.1994.1127
发表时间：
1994
期刊：
Journal of magnetic resonance. Series B
影响因子：
--
作者：
Schurr,JM;Babcock,HP;Fujimoto,BS
通讯作者：
Fujimoto,BS
蛋白质内部动力学缓慢：NMR 弛豫色散光谱在 T4 溶菌酶空腔突变体中甲基的应用。
影响因子：
15
作者：
Mulder,FransAA;Hon,Bin;Mittermaier,Anthony;Dahlquist,FrederickW;Kay,LewisE
通讯作者：
Kay,LewisE
影响因子：
15
作者：
Mulder, FAA;Skrynnikov, NR;Kay, LE
通讯作者：
Kay, LE
影响因子：
5.6
作者：
Wright, PE;Dyson, HJ
通讯作者：
Dyson, HJ