Journal article

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

Xiaojun Yuan, Matthew D Johnson, Jing Zhang, Alvin W Lo, Mark A Schembri, Lakshmi C Wijeyewickrema, Robert N Pike, Gerard HM Huysmans, Ian R Henderson, Denisse L Leyton

Nat Commun | Published : 2018

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 molecules catalyze the assembly of the autotransporter β-barrel domain. However, how the passenger domain folds into its functional form is poorly understood. Here we use mutational analysis on the autotransporter Pet to show that the β-hairpin structure of the fifth extracellular loop of the β-barrel domain has a crucial role for passenger domai..

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