Journal
PLOS ONE
Volume 8, Issue 8, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0073572
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Funding
- Agence Nationale de la Recherche, ANR DYN FHAC (France)
- Fonds National de la Recherche Scientifique (Belgium) INSERM
- CNRS
- Universite Lille Nord de France (France)
- Region Rhone-Alpes (France)
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The parallel beta helix is a common fold among extracellular proteins, however its mechanical properties remain unexplored. In Gram-negative bacteria, extracellular proteins of diverse functions of the large 'TpsA' family all fold into long beta helices. Here, single-molecule atomic force microscopy and steered molecular dynamics simulations were combined to investigate the mechanical properties of a prototypic TpsA protein, FHA, the major adhesin of Bordetella pertussis. Strong extension forces were required to fully unfold this highly repetitive protein, and unfolding occurred along a stepwise, hierarchical process. Our analyses showed that the extremities of the beta helix unfold early, while central regions of the helix are more resistant to mechanical unfolding. In particular, a mechanically resistant subdomain conserved among TpsA proteins and critical for secretion was identified. This nucleus harbors structural elements packed against the beta helix that might contribute to stabilizing the N-terminal region of FHA. Hierarchical unfolding of the beta helix in response to a mechanical stress may maintain beta-helical portions that can serve as templates for regaining the native structure after stress. The mechanical properties uncovered here might apply to many proteins with beta-helical or related folds, both in prokaryotes and in eukaryotes, and play key roles in their structural integrity and functions.
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