Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima
Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima
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DOI：
10.1016/s0969-2126(01)00706-7
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发表时间：
2002-02-01
期刊：
影响因子：
5.7
通讯作者：
Stock, AM
中科院分区：
文献类型：
--
作者：
Buckler, DR;Zhou, YC;Stock, AM
双组分系统是原核生物使用的主要信号转导策略，涉及从传感器组氨酸激酶(HK)到细胞内反应调节蛋白(RR)的磷酸转导，后者通常充当转录调节因子。RRs是一种模块化蛋白，通常由一个保守的调节域和一个附加的DNA结合效应域组成，后者起着磷酸化激活开关的作用。一个Thermotoga maritima转录因子DrrD的晶体结构已经在1.5埃分辨率下被测定，这为RRs的OmpR/Phob亚家族的全长成员提供了第一个结构信息。在调节域的α5和效应域的反平行薄片之间出现小的域间界面。在非磷酸化蛋白中缺乏广泛的界面，这使得DrrD有别于其他结构特征的多域RRs，并暗示了一种不同的域间调控模式。
Two-component systems, the predominant signal transduction strategy used by prokaryotes, involve phosphorelay from a sensor histidine kinase (HK) to an intracellular response regulator protein (RR) that typically acts as a transcription regulator. RRs are modular proteins, usually composed of a conserved regulatory domain, which functions as a phosphorylation-activated switch, and an attached DNA binding effector domain. The crystal structure of a Thermotoga maritima transcription factor, DrrD, has been determined at 1.5 Angstrom resolution, providing the first structural information for a full-length member of the OmpR/PhoB subfamily of RRs. A small interdomain interface occurs between alpha5 of the regulatory domain and an antiparallel sheet of the effector domain. The lack of an extensive interface in the unphosphorylated protein distinguishes DrrD from other structurally characterized multidomain RRs and suggests a different mode of interdomain regulation.