Structure of PAS-linked histidine kinase and the response regulator complex.
Structure of PAS-linked histidine kinase and the response regulator complex.
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DOI：
10.1016/j.str.2009.07.016
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发表时间：
2009-10
期刊：
影响因子：
5.7
通讯作者：
S. Yamada;H. Sugimoto;Miki Kobayashi;A. Ohno;Hiro Nakamura;Y. Shiro
中科院分区：
文献类型：
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作者：
S. Yamada;H. Sugimoto;Miki Kobayashi;A. Ohno;Hiro Nakamura;Y. Shiro
研究了海洋热藓双组分信号转导系统中感觉组氨酸激酶（HK）及其同源反应调节因子（RR）复合物的结构。这是通过将孤立HK域和RR的高分辨率结构拟合到HK/RR复合物晶体的电子密度图（3.8 Å分辨率）上实现的。基于结构信息，我们评估了结构域间和分子间相互作用在细胞质pas连接的HK和RR系统的信号转导中的作用，特别是o2传感器FixL/FixJ系统。HK的pas传感器结构域与同一多肽链的催化结构域通过形成结构域间β片相互作用。经核磁共振证实HK与RR的相互作用位点适合于磷酸化基团的分子间转移反应，表明所观察到的相互作用对HK去磷酸化磷酸化-RR的磷酸酶活性是重要的。
We determined the structure of the complex of the sensory histidine kinase (HK) and its cognate response regulator (RR) in the two-component signal transduction system ofThermotoga maritima. This was accomplished by fitting the high-resolution structures of the isolated HK domains and the RR onto the electron density map (3.8 Å resolution) of the HK/RR complex crystal. Based on the structural information, we evaluated the roles of both interdomain and intermolecular interactions in the signal transduction of the cytosolic PAS-linked HK and RR system, in particular the O2-sensor FixL/FixJ system. The PAS-sensor domain of HK interacts with the catalytic domain of the same polypeptide chain by creating an interdomain β sheet. The interaction site between HK and RR, which was confirmed by NMR, is suitable for the intermolecular transfer reaction of the phosphoryl group, indicating that the observed interaction is important for the phosphatase activity of HK that dephosphorylates phospho-RR.