The natural transformation system of the thermophilic bacterium Thermus thermophilus is one of the most efficient DNA transport systems in terms of DNA uptake rate and promiscuity. The DNA transporter of T. thermophilus plays an important role in interdomain DNA transfer in hot environments. PilF is the traffic ATPase that provides the energy for the assembly of the DNA translocation machinery and the functionally linked type IV pilus system in T. thermophilus. In contrast to other known traffic ATPases, the N-terminal region of PilF harbors three consecutive domains with homology to general secretory pathway II (GSPII) domains. These GSPII-like domains influence pilus assembly, twitching motility and transformation efficiency. A structural homolog of the PilF GSPII-like domains, the N-terminal domain of the traffic ATPase MshE from Vibrio cholerae, was recently crystallized in complex with the bacterial second messenger c-di-GMP. In order to study the consequences of c-di-GMP binding on the three-dimensional architecture of PilF, we initiated structural studies on the PilF GSPII-like domains. Here, we present the ¹H, ¹³C and ¹⁵N chemical shift assignments for the isolated PilF GSPII-C domain from T. thermophilus in complex with c-di-GMP. In addition, the structural dynamics of the complex was investigated in an {¹H},¹⁵N-hetNOE experiment.

中文翻译：

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与C-di-GMP结合的嗜热栖热菌PilF ATPase GSPII-C结构域的NMR共振分配。

就DNA的摄取率和滥交性而言，嗜热的嗜热菌Thermus thermophilus的天然转化系统是最有效的DNA转运系统之一。的DNA转运嗜热场在热的环境中域间DNA转移中起重要作用。PilF是运输性ATP酶，可为嗜热嗜热菌中的DNA易位机制和功能性连接的IV型菌毛系统的组装提供能量。。与其他已知的交通ATP酶相反，PilF的N端区域包含三个与一般分泌途径II（GSPII）域同源的连续域。这些类似GSPII的域会影响菌毛的组装，抽动力和转化效率。PilF GSPII样域的结构同源物，即来自霍乱弧菌的交通ATPase MshE的N端域，最近与细菌第二信使c-di-GMP形成了结晶。为了研究c-di-GMP结合对PilF三维结构的影响，我们启动了对PilF GSPII样结构域的结构研究。在这里，我们介绍¹ H，¹³ C和¹⁵与嗜热链球菌分离的PilF GSPII-C结构域与c-di-GMP结合的N个化学位移分配。此外，在{ ¹ H}，¹⁵ N-hetNOE实验中研究了复合物的结构动力学。