Postel Sandra, Deredge Daniel, Bonsor Daniel A, Yu Xiong, Diederichs Kay, Helmsing Saskia, Vromen Aviv, Friedler Assaf, Hust Michael, Egelman Edward H, Beckett Dorothy, Wintrode Patrick L, Sundberg Eric J
Institute of Human Virology, University of Maryland School of Medicine, Baltimore, United States.
Department of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, United States.
Elife. 2016 Sep 24;5:e18857. doi: 10.7554/eLife.18857.
Flagella are crucial for bacterial motility and pathogenesis. The flagellar capping protein (FliD) regulates filament assembly by chaperoning and sorting flagellin (FliC) proteins after they traverse the hollow filament and exit the growing flagellum tip. In the absence of FliD, flagella are not formed, resulting in impaired motility and infectivity. Here, we report the 2.2 Å resolution X-ray crystal structure of FliD from , the first high-resolution structure of any FliD protein from any bacterium. Using this evidence in combination with a multitude of biophysical and functional analyses, we find that FliD exhibits unexpected structural similarity to other flagellar proteins at the domain level, adopts a unique hexameric oligomeric state, and depends on flexible determinants for oligomerization. Considering that the flagellin filaments on which FliD oligomers are affixed vary in protofilament number between bacteria, our results suggest that FliD oligomer stoichiometries vary across bacteria to complement their filament assemblies.
鞭毛对于细菌的运动性和致病性至关重要。鞭毛帽蛋白(FliD)通过在鞭毛蛋白(FliC)穿过中空的鞭毛丝并离开生长中的鞭毛尖端后对其进行伴侣介导和分选,来调节鞭毛丝的组装。在没有FliD的情况下,鞭毛无法形成,导致运动性和感染性受损。在此,我们报告了来自[具体细菌名称]的FliD的2.2埃分辨率X射线晶体结构,这是来自任何细菌的任何FliD蛋白的首个高分辨率结构。结合大量生物物理和功能分析的证据,我们发现FliD在结构域水平上与其他鞭毛蛋白表现出意想不到的结构相似性,采用独特的六聚体寡聚状态,并且寡聚化依赖于灵活的决定因素。鉴于FliD寡聚体所附着的鞭毛蛋白丝在不同细菌中的原丝数量不同,我们的结果表明,FliD寡聚体的化学计量在不同细菌中有所不同,以补充它们的鞭毛丝组装。