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首页> 外文期刊>Biochemistry >High-resolution solution structure of the beryllofluoride-activated NtrC receiver domain
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High-resolution solution structure of the beryllofluoride-activated NtrC receiver domain

机译：氟化铍活化的NtrC受体域的高分辨率溶液结构

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摘要

Bacterial receiver domains mediate the cellular response to environmental changes through conformational changes induced by phosphorylation of a conserved aspartate residue. While the structures of several activated receiver domains have recently been determined, there is substantial variation in the conformational changes occurring upon activation. Here we present the high-resolution structure of the activated NtrC receiver domain (BeF3--NtrCr Complex) determined using NMR data, including residual dipolar couplings, yielding a family of structures with a backbone rmsd of 0.57 +/- 0.08 Angstrom, which is compared with the previous lower-resolution structure of the phosphorylated protein. Both phosphorylation and beryllofluoride addition induce a shift in register and an axial rotation of alpha-helix 4. In this high-resolution structure, we are able to observe a concerted change in the positions of Thr82 and Tyr101; this correlated change in two conserved residues (termed Y-T coupling) has been considered a general feature of the conformational change in receiver domains upon activation. In NtrC, this correlated side chain shift, leading to the helix reorientation, is distinctly different from the smaller reorganization seen in other activated receiver domains, and involves numerous other residues which do not participate in conformational changes seen in the other systems. Titration of the activated receiver domain with peptides from the NtrC ATPase domain provides direct evidence for interactions on the rearranged face of the receiver domain, which are likely to be responsible for enabling assembly into the active aggregate. Analysis of the active structure also suggests that His84 may play a role in controlling the phosphate hydrolysis rate. [References: 59]
机译：细菌受体结构域通过保守的天冬氨酸残基的磷酸化诱导的构象变化介导细胞对环境变化的响应。尽管最近已确定了几个激活的受体域的结构，但是在激活时发生的构象变化有很大的变化。在这里，我们介绍了使用NMR数据确定的，激活的NtrC受体域（BeF3--NtrCr配合物）的高分辨率结构，包括残留的偶极耦合，产生了主链均方根值为0.57 +/- 0.08埃的结构族。与以前的磷酸化蛋白的低分辨率结构相比。磷酸化和铍氟化物的添加均引起套准移位和α螺旋4的轴向旋转。在这种高分辨率结构中，我们能够观察到Thr82和Tyr101的位置发生一致的变化。两个保守残基的这种相关变化（称为Y-T偶联）已被认为是激活后受体域构象变化的一般特征。在NtrC中，这种相关的侧链移位导致螺旋重新定向，与在其他激活的受体域中看到的较小重组明显不同，并且涉及许多其他残基，这些残基不参与在其他系统中看到的构象变化。用来自NtrC ATPase结构域的肽滴定活化的受体结构域，可为受体结构域重排面上的相互作用提供直接证据，这很可能导致组装成活性聚集体。活性结构的分析还表明，His84可能在控制磷酸盐水解速率中起作用。 [参考：59]

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