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首页> 外文期刊>Journal of Molecular Biology >Unraveling Allostery in a Knotted Minimal Methyltransferase by NMR Spectroscopy
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Unraveling Allostery in a Knotted Minimal Methyltransferase by NMR Spectroscopy

机译：通过NMR光谱解开亚甲基转移酶中的解开象生物

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The methyltransferases that belong to the SpoU-TrmD family contain trefoil knots in their backbone fold. Recent structural dynamic and binding analyses of both free and bound homologs indicate that the knot within the polypeptide backbone plays a significant role in the biological activity of the molecule. The knot loops form the S-adenosyl-methionine (SAM)-binding pocket as well as participate in SAM binding and catalysis. Knots contain both at once a stable core as well as moving parts that modulate long-range motions. Here, we sought to understand allosteric effects modulated by the knotted topology. Uncovering the residues that contribute to these changes and the functional aspects of these protein motions are essential to understanding the interplay between the knot, activation of the methyltransferase, and the implications in RNA interactions. The question we sought to address is as follows: How does the knot, which constricts the backbone as well as forms the SAM-binding pocket with its three distinctive loops, affect the binding mechanism? Using a minimally tied trefoil protein as the framework for understanding the structure-function roles, we offer an unprecedented view of the conformational mechanics of the knot and its relationship to the activation of the ligand molecule. Focusing on the biophysical characterization of the knot region by NMR spectroscopy, we identify the SAM-binding region and observe changes in the dynamics of the loops that form the knot. Importantly, we also observe long-range allosteric changes in flanking helices consistent with winding/unwinding in helical propensity as the knot tightens to secure the SAM cofactor. (C) 2020 Published by Elsevier Ltd.
机译：属于SPOU-TRMD系列的甲基转移酶含有在其骨架上的三叶刀。自由和结合同源物的最近结构动态和结合分析表明，多肽骨架内的结在分子的生物活性中起着重要作用。结环形形成S-腺苷 - 蛋氨酸（SAM） - 缠结口袋以及参与SAM结合和催化。结在一起含有稳定的核心以及调制远程运动的运动部件。在这里，我们试图了解被打结拓扑调制的变构效果。揭开有助于这些变化的残基和这些蛋白质运动的功能方面对于了解结结，激活甲基转移酶的相互作用以及RNA相互作用的影响是必要的。我们寻求地址的问题如下：结的结是如何限制骨干的结，以及用其三个独特的环形形成Sam绑定口袋，影响绑定机制？使用微量绑定的三叶蛋白作为理解结构功能作用的框架，我们提供了前所未有的结合力学的视图，以及其与配体分子的激活的关系。专注于通过NMR光谱的结区域的生物物理表征，我们识别SAM绑定区域，并观察形成结的环的动态的变化。重要的是，我们还观察到侧翼螺旋中的长距离构建变化，与螺旋倾斜的绕组/展开，因为结紧固以固定SAM Cofactor。 （c）2020由elestvier有限公司发布

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