Structure of the periplasmic domain of SflA involved in spatial regulation of the flagellar biogenesis of Vibrio reveals a TPR/SLR -like fold.
Structure of the periplasmic domain of SflA involved in spatial regulation of the flagellar biogenesis of Vibrio reveals a TPR/SLR -like fold.
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DOI：
10.1093/jb/mvz027
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发表时间：
2019-08
影响因子：
2.7
通讯作者：
M. Sakuma;S. Nishikawa;S. Inaba;T. Nishigaki;S. Kojima;M. Homma;K. Imada
中科院分区：
文献类型：
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作者：
M. Sakuma;S. Nishikawa;S. Inaba;T. Nishigaki;S. Kojima;M. Homma;K. Imada
细菌进化出了各种类型的鞭毛，这是一种细菌运动的细胞器，以适应它们的栖息地环境。鞭毛的数量和空间排列被精确控制，以优化每种类型鞭毛系统的性能。溶藻弧菌在细胞杆上有一根可供游泳的有鞘的鞭毛。SflA是一种防止有鞘鞭毛形成的调节蛋白，由N-末端周质区域、跨膜螺旋和C-末端细胞质区域组成。虽然细胞质区域被认为是抑制胞周生长所必需的，但N-末端区域的作用仍不清楚。我们在这里测定了SflA的N-末端周质区域(SflAN)的结构，分辨率为1.9？SflAN的核心形成一个具有四肽重复序列(TPR)/类Sel1重复序列(SLR)基序的结构域交换二聚体，它经常存在于各种蛋白质中负责蛋白质相互作用的结构域中。结构相似性和基于结构的突变分析表明，SflA通过SflAN与未知的伴侣蛋白结合，结合信号对SflA功能的精确调控具有重要意义。
Bacteria have evolved various types of flagellum, an organella for bacterial motility, to adapt to their habitat environments. The number and the spatial arrangement of the flagellum are precisely controlled to optimize performance of each type of the flagellar system. Vibrio alginolyticus has a single sheathed flagellum at the cell pole for swimming. SflA is a regulator protein to prevent peritrichous formation of the sheathed flagellum, and consists of an N-terminal periplasmic region, a transmembrane helix, and a C-terminal cytoplasmic region. Whereas the cytoplasmic region has been characterized to be essential for inhibition of the peritrichous growth, the role of the N-terminal region is still unclear. We here determined the structure of the N-terminal periplasmic region of SflA (SflAN) at 1.9 Å resolution. The core of SflAN forms a domain-swapped dimer with tetratricopeptide repeat (TPR)/Sel1-like repeats (SLR) motif, which is often found in the domains responsible for protein-protein interaction in various proteins. The structural similarity and the following mutational analysis based on the structure suggest that SflA binds to unknown partner protein by SflAN and the binding signal is important for the precise control of the SflA function.