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 H.M. Huysmans, Ian R. Henderson, Denisse L. Leyton*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

19 Citations (Scopus)


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 domain folding into a β-helix. Bioinformatics and structural analyses, and mutagenesis of a homologous autotransporter, suggest that this function is conserved among autotransporter proteins with β-helical passenger domains. We propose that the autotransporter β-barrel domain is a folding vector that nucleates folding of the passenger domain.

Original languageEnglish
Article number1395
JournalNature Communications
Issue number1
Publication statusPublished - 1 Dec 2018


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