Heck D V, Trus B L, Steven A C
Laboratory of Structural Biology, National Institutes of Health, Bethesda, Maryland, 20892, USA.
J Struct Biol. 1996 Mar-Apr;116(2):264-9. doi: 10.1006/jsbi.1996.0041.
We describe the helical structure of Bordetella pertussis fimbriae of serotype 3/6 as determined to a resolution of approximately 2.5 nm by three-dimensional reconstruction of negatively stained electron micrographs. The fimbria has a distinctly polar structure whose axial repeat of 13 nm contains five copies of the fim3 gene product (22 kDa) in two complete turns. These subunits are connected by interactions along the fimbrial backbone which, unlike other classes of bacterial fimbriae, has no axial channel. Its outer diameter is approximately 5.7 nm, and the most pronounced feature is a radially protruding domain that gives the fimbria its characteristic serrated appearance. Serotype 2 fimbriae, composed of the fim2 subunit which is 60% homologous with fim3, have essentially the same quaternary structure. These observations are discussed in relation to fimbrial phase variation and structure-based classification of fimbriae/pili.
我们描述了3/6血清型百日咳博德特氏菌菌毛的螺旋结构,该结构通过对负染电子显微镜照片进行三维重建,分辨率约为2.5纳米。菌毛具有明显的极性结构,其13纳米的轴向重复序列在两整圈中包含五个fim3基因产物(22 kDa)拷贝。这些亚基通过沿菌毛主干的相互作用相连,与其他类别的细菌菌毛不同,该菌毛没有轴向通道。其外径约为5.7纳米,最显著的特征是一个径向突出的结构域,使菌毛呈现出特有的锯齿状外观。由与fim3有60%同源性的fim2亚基组成的2型菌毛,其四级结构基本相同。结合菌毛相变异和基于结构的菌毛/菌毛蛋白分类对这些观察结果进行了讨论。