Full-Length Structure of a Sensor Histidine Kinase Pinpoints Coaxial Coiled Coils as Signal Transducers and Modulators
Full-Length Structure of a Sensor Histidine Kinase Pinpoints Coaxial Coiled Coils as Signal Transducers and Modulators
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DOI：
10.1016/j.str.2013.04.024
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发表时间：
2013-07-02
期刊：
影响因子：
5.7
通讯作者：
Moeglich, Andreas
中科院分区：
文献类型：
--
作者：
Diensthuber, Ralph P.;Bommer, Martin;Moeglich, Andreas
双组分系统（TCS），其中包括传感器组氨酸激酶（SHK）和响应调节蛋白，代表了原核生物的主要战略，通过它来感知和响应不断变化的环境。尽管至关重要的生物重要性，缺乏完整的SHK结构包含传感器和效应器模块。在这里，我们报告了全长晶体结构的工程，二聚体，蓝光调节SHK YF 1在2.3埃的分辨率，其中两个N-末端光氧电压（LOV）光传感器连接的卷曲螺旋的C-末端效应模块。第二个同轴卷曲螺旋来自N-末端的LOV光电传感器和插入它们之间的关键调制光调节：在这个卷曲螺旋内的单个突变衰减，甚至反转的TCS的信号响应。在YF 1中鉴定的结构基序在信号受体中重现，并且潜在的信号传导原理和机制可能在具有不同生物活性的可溶性和跨膜、原核和真核信号受体之间广泛共享。
Two-component systems (TCSs), which comprise sensor histidine kinases (SHK) and response-regulator proteins, represent the predominant strategy by which prokaryotes sense and respond to a changing environment. Despite paramount biological importance, a dearth exists of intact SHK structures containing both sensor and effector modules. Here, we report the full-length crystal structure of the engineered, dimeric, blue-light-regulated SHK YF1 at 2.3 angstrom resolution, in which two N-terminal light-oxygen-voltage (LOV) photosensors are connected by a coiled coil to the C-terminal effector modules. A second coaxial coiled coil derived from the N-termini of the LOV photosensors and inserted between them crucially modulates light regulation: single mutations within this coiled coil attenuate or even invert the signal response of the TCS. Structural motifs identified in YF1 recur in signal receptors, and the underlying signaling principles and mechanisms may be widely shared between soluble and transmembrane, prokaryotic, and eukaryotic signal receptors of diverse biological activity.