Biological insights from structures of two-component proteins.
Biological insights from structures of two-component proteins.
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DOI：
10.1146/annurev.micro.091208.073214
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发表时间：
2009
影响因子：
10.5
通讯作者：
Stock AM
中科院分区：
文献类型：
--
作者：
Gao R;Stock AM
基于从组氨酸蛋白激酶到反应调节蛋白的磷酸转移的双组分信号转导是将环境刺激耦合到细菌适应性反应的普遍策略。在组氨酸激酶和反应调节剂中，具有保守结构和生物化学活性的模块化结构域在刺激物存在下或在磷酸化后采用不同的构象状态，使得能够基于由不同结构域排列赋予的抑制性和/或活化性蛋白质-蛋白质相互作用的多种调控机制。这篇综述总结了一些最近的结构工作，提供了深入了解细菌组氨酸激酶和反应调节剂的功能。特别强调的是放在识别功能，预计将被保存在不同的双组分蛋白质从那些预计不同的，与定义的程度，以前的特点，双组分蛋白质的知识可以应用到新发现的系统的目标。
Two-component signal transduction based on phosphotransfer from a histidine protein kinase to a response regulator protein is a prevalent strategy for coupling environmental stimuli to adaptive responses in bacteria. In both histidine kinases and response regulators, modular domains with conserved structures and biochemical activities adopt different conformational states in the presence of stimuli or upon phosphorylation, enabling a diverse array of regulatory mechanisms based on inhibitory and/or activating protein-protein interactions imparted by different domain arrangements. This review summarizes some of the recent structural work that has provided insight to the functioning of bacterial histidine kinases and response regulators. Particular emphasis is placed on identifying features that are expected to be conserved among different two-component proteins from those that are expected to differ, with the goal of defining the extent to which knowledge of previously characterized two-component proteins can be applied to newly discovered systems.
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