Journal article
Molecular basis for the folding of β-helical autotransporter passenger domains
X Yuan, MD Johnson, J Zhang, AW Lo, MA Schembri, LC Wijeyewickrema, RN Pike, GHM Huysmans, IR Henderson, DL Leyton
Nature Communications | NATURE PORTFOLIO | 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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Awarded by Australian Respiratory Council
Funding Acknowledgements
We thank Alex Joule and Anthony Newman for technical assistance, Trevor Lithgow and lain Hay for providing the E coli BW25113 Delta ompT strain, John Carver for access to the Chirascan spectrometer, as well as Susan Howitt for critical comments on the manuscript. We gratefully acknowledge support of the Australian Research Council (ARC) for research funding through the ARC Discovery Project grant DP160103294 (to D.L.L. and I.R.H.). M.A.S. is a National Health and Medical Research Council Senior Research Fellow (APP1106930), G.H.M.H. is supported by a Global Marie-Curie Fellowship (EU project 660083), and D.L.L. is an ARC Future Fellow (FT150100452).