Molecular mechanism of the construction of the bacterial flagellar rod.

在这项研究中，我们确定了FlgJ的C-末端片段的晶体结构，它具有溶菌酶活性，并揭示了肽聚糖水解的分子机制。FlgJ的活性中心结构和整体折叠类似于鸡蛋白色溶菌酶。有趣的是，FlgJ的活性被非常少量的阳离子强烈抑制。我们通过向纯化的鞭毛钩中加入杆蛋白来重建远端杆。此外，我们阐明了杆和FlgD，钩帽蛋白之间的相互作用。

In this study, we determined the crystal structure of a C-terminal fragment of FlgJ, which has a muramidase activity, and revealed the molecular mechanism of the peptidoglican hydrolysis. The active site structure and the overall folding of FlgJ resemble those of hen egg white lysozyme. Interestingly, the activity of FlgJ is strongly inhibited by a very small amount of cation. We reconstituted distal rod by adding rod proteins to the purified flagellar hook. Moreover, we elucidated the interaction between the rod and FlgD, the hook cap protein.