The crystal structure of YycH involved in the regulation of the essential YycFG two-component system in Bacillus subtilis reveals a novel tertiary structure.
The crystal structure of YycH involved in the regulation of the essential YycFG two-component system in Bacillus subtilis reveals a novel tertiary structure.
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参与枯草芽孢杆菌中必需的 YycFG 双组分系统调节的 YycH 晶体结构揭示了一种新颖的三级结构。
DOI：
10.1110/ps.052064406
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发表时间：
2006
期刊：
影响因子：
--
通讯作者：
Varughese,KottayilI
中科院分区：
文献类型：
--
作者：
Szurmant,Hendrik;Zhao,Haiyan;Mohan,MichaelA;Hoch,JamesA;Varughese,KottayilI
枯草芽孢杆菌YycFG双组分信号转导系统对于细胞活力至关重要，而YycH蛋白是控制其活性的调节回路的一部分。 YycH 的晶体结构通过双波长硒反常色散数据求解，并使用 2.3 Å 数据精修至 R 因子为 25.2%。该分子由三个域组成，具有新颖的三维结构。 N 末端结构域具有钙结合位点，中心结构域包含两个保守的环区域。
TheBacillus subtilisYycFG two‐component signal transduction system is essential for cell viability, and the YycH protein is part of the regulatory circuit that controls its activity. The crystal structure of YycH was solved by two‐wavelength selenium anomalous dispersion data, and was refined using 2.3 Å data to anR‐factor of 25.2%. The molecule is made up of three domains, and has a novel three‐dimensional structure. The N‐terminal domain features a calcium binding site and the central domain contains two conserved loop regions.