Dimerization allows DNA target site recognition by the NarL response regulator
Dimerization allows DNA target site recognition by the NarL response regulator
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DOI：
10.1038/nsb845
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发表时间：
2002-10-01
期刊：
影响因子：
--
通讯作者：
Dickerson, RE
中科院分区：
文献类型：
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作者：
Maris, AE;Sawaya, MR;Dickerson, RE
双组分信号转导系统是原核生物中常见的模块化磷酸化调节途径。在大肠杆菌NarL信号输出结构域与DNA结合的共晶结构中，我们观察了NarL家族的双组分反应调节剂如何结合DNA。DNA识别伴随着一个新的二聚化界面的形成，这可能只发生在全长蛋白质通过一个大的分子内结构域重排。DNA是通过溶剂化、货车范德华力和固有的DNA变形性的协同作用来识别的，而不是主要由大沟氢键决定的。这些微妙的力量允许一个小的DNA结合结构域扰乱B的DNA螺旋，导致主要的DNA弯曲和从B-到A-形式的DNA在结合位点的过渡，在识别螺旋上的缬氨酸意外地与极性大沟底相互作用。
Two-component signal transduction systems are modular phosphorelay regulatory pathways common in prokaryotes. In the co-crystal structure of the Escherichia coli NarL signal output domain bound to DNA, we observe how the NarL family of two-component response regulators can bind DNA. DNA recognition is accompanied by the formation of a new dimerization interface, which could occur only in the full-length protein via a large intramolecular domain rearrangement. The DNA is recognized by the concerted effects of solvation, van der Waals forces and inherent DNA deformability, rather than determined primarily by major groove hydrogen bonding. These subtle forces permit a small DNA-binding domain to perturb the DNA helix, leading to major DNA curvature and a transition from B- to A-form DNA at the binding site, where valine on the recognition helix interacts unexpectedly with the polar major groove floor.