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

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

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)
148 Downloads (Pure)


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 - 11 Apr 2018


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