SecDF function and roles of the proton motive force in protein translocation

在细菌中，蛋白质的跨膜易位是由膜整合成分（SecDF）刺激的。然而，其分子机制尚不清楚。在本研究中，我们以3.3 A的分辨率测定了Thermus thermophilusSecDF的晶体结构，并根据结构信息进行了多项生化分析。最后，我们提出了一个工作假设，即SecDF作为一个膜集成马达，由PMF驱动，实现了Sec机制不依赖于eap的全蛋白易位能力

In bacteria, protein translocation across the membrane is stimulated by membrane-integrated components, SecDF. However, itsmolecular mechanisms remainunknown. In this study, we determined the crystal structure of Thermus thermophilusSecDF at 3.3 A resolutionand carried out a number of biochemical analysis based on the structural information.Finally, we propose a working hypothesis that SecDF functions as a membrane-integrated motor, powered by PMF, to achieveATP-independent full protein translocation ability of the Sec machinery