Abstract
The membrane protein SecDF, belonging to the RNDsuperfamily, enhances protein translocation atthe extracytoplasmic side using a proton gradient.Here, we report the crystal structure of SecDF in a form we named Super-membrane-facing (Super F) form, demonstrating a β-barrel architecture instead of the previously reported β-sheet structure. Through this structural insight and supporting results of an invivo crosslinking experiment, we propose a remote coupling model in which a structural change of the transmembrane region drives a functional, extracytoplasmic conformational transition.
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