PDF(Pubmed)
Abstract：
The GTPase FlhF, a signal recognition particle (SRP)-type enzyme, is pivotal for spatial-numerical control and bacterial flagella assembly across diverse species, including pathogens. This study presents the X-ray structure of FlhF in its GDP-bound state at a resolution of 2.28 Å. The structure exhibits the classical N- and G-domain fold, consistent with related SRP GTPases such as Ffh and FtsY. Comparative analysis with GTP-loaded FlhF elucidates the conformational changes associated with GTP hydrolysis. These topological reconfigurations are similarly evident in Ffh and FtsY, and play a pivotal role in regulating the functions of these hydrolases.
摘要：
GTPaseFlhF,信号识别粒子（SRP）型酶，对于不同物种的空间数字控制和细菌鞭毛组装至关重要，包括病原体。这项研究以2.28的分辨率呈现了FlhF在GDP束缚状态下的X射线结构。该结构表现出经典的N-和G-结构域折叠，与Ffh和FtsY等相关SRPGTP酶一致。与GTP负载的FlhF的比较分析阐明了与GTP水解相关的构象变化。这些拓扑重新配置在Ffh和FtsY中同样明显，并在调节这些水解酶的功能中起关键作用。
