Molecular basis for the folding of β-helical autotransporter passenger domains
Research output: Contribution to journal › Article › peer-review
Colleges, School and Institutes
- Research School of Biology, Australian National University, Canberra, ACT, 0200, Australia.
- Australian Infectious Disease Research Centre, The University of Queensland, Brisbane, QLD, 4072, Australia.
- Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC, 3086, Australia.
- Department of Physiology and Biophysics, Weill Cornell Medicine, New York, NY, 10065, USA.
- Institute of Microbiology and Infection, University of Birmingham, Birmingham, B15 2TT, UK. email@example.com.
- Medical School, Australian National University, Canberra, ACT, 0200, Australia. firstname.lastname@example.org.
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.
|Publication status||Published - 11 Apr 2018|