Abstract
The ATPase SecA converts energy generated from ATP hydrolysis to drive conformational change in the highly conserved Sec complex which in turn transports proteins from the cytoplasm to the periplasm in bacteria. The mechanism by which proteins are transported in this manner is still poorly understood. Here, we use single-molecule FRET (smFRET) to study the rates of conformational change induced in the Sec complex during each stage of its hydrolysis cycle and connect this to a larger picture of how SecA allosterically modulates the membrane bound molecular machine that is the Sec translocon.
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