Molecular basis for the folding of β-helical autotransporter passenger domains

Abstract

Bacterial autotransporters comprise a C-terminal β-barrel domain, which must be correctly folded and inserted into the outer membrane to facilitate translocation of the N-terminal passenger domain to the cell exterior. Once at the surface, the passenger domains of most autotransporters are folded into an elongated β-helix. In a cellular context, key… (More)
DOI: 10.1038/s41467-018-03593-2

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