Abstract
The autotransporters are a family of bacterial outer membrane proteins that are characterised by three functional domains: an N-terminal signal sequence, a central passenger domain, and a C-terminal transmembrane β-barrel domain. Using molecular dynamics simulations we explore the structural dynamics and membrane interactions of the β-barrel domains from six autotransporters: BrkA, NalP, EspP, EstA, Hia and Hbp. The β-barrel domain has been proposed to aid in the translocation of the passenger domain across the outer membrane.
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