Crystal structure of the histidine‐containing phosphotransfer protein ZmHP2 from maize
Crystal structure of the histidine‐containing phosphotransfer protein ZmHP2 from maize
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DOI：
10.1110/ps.041076905
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发表时间：
2005-01
期刊：
影响因子：
8
通讯作者：
H. Sugawara;Y. Kawano;T. Hatakeyama;T. Yamaya;N. Kamiya;H. Sakakibara
中科院分区：
文献类型：
--
作者：
H. Sugawara;Y. Kawano;T. Hatakeyama;T. Yamaya;N. Kamiya;H. Sakakibara
在高等植物中，组氨酸-天冬氨酸磷酸传递（双组分系统）参与激素信号传导和胁迫反应。在这些系统中，含组氨酸的磷酸转移（HPt）蛋白介导从感觉组氨酸激酶到反应调节剂的信号传递，包括整合几个信号通路或分支到不同的通路。我们已经确定了玉米HPt蛋白，ZmHP 2，在2.2 μ m分辨率的晶体结构。ZmHP 2有六个α螺旋，C末端有一个四螺旋束，这是HPt结构域中常见的特征。在ZmHP 2中，几乎所有的植物HPt蛋白的保守残基都围绕着这个组氨酸，可能形成了组氨酸激酶或响应调节器的受体结构域的对接界面。ZmHP 2的Arg 102在植物HPt蛋白中是保守的碱性残基。在细菌中，它被谷氨酰胺或谷氨酸取代，与磷酸化组氨酸的Nδ原子形成氢键。它可能在ZmHP 2与接收域的复合物形成中起关键作用。
In higher plants, histidine‐aspartate phosphorelays (two‐component system) are involved in hormone signaling and stress responses. In these systems, histidine‐containing phosphotransfer (HPt) proteins mediate the signal transmission from sensory histidine kinases to response regulators, including integration of several signaling pathways or branching into different pathways. We have determined the crystal structure of a maize HPt protein, ZmHP2, at 2.2 Å resolution. ZmHP2 has six α‐helices with a four‐helix bundle at the C‐terminus, a feature commonly found in HPt domains. In ZmHP2, almost all of the conserved residues among plant HPt proteins surround this histidine, probably forming the docking interface for the receiver domain of histidine kinase or the response regulator. Arg102 of ZmHP2 is conserved as a basic residue in plant HPt proteins. In bacteria, it is replaced by glutamine or glutamate that form a hydrogen bond to Nδ atoms of the phospho‐accepting histidine. It may play a key role in the complex formation of ZmHP2 with receiver domains.