Rok 2017

• Role of the disulfide bond in stabilizing and folding of the fimbrial protein DraE from uropathogenic Escherichia coli

  Publikacja

  • J. Pilipczuk
  • B. Zalewska-Piątek
  • P. Bruździak
  • J. Czub
  • M. Wieczór
  • M. Olszewski
  • M. Wanarska
  • B. Nowicki
  • D. Augustin-Nowacka
  • R. Piątek

  - JOURNAL OF BIOLOGICAL CHEMISTRY - Rok 2017

  Dr fimbriae are homopolymeric adhesive organelles of uropathogenic Escherichia coli composed of DraE subunits, responsible for the attachment to host cells. These structures are characterized by enormously high stability resulting from the structural properties of an Ig-like fold of DraE. One feature of DraE and other fimbrial subunits that makes them peculiar among Ig-like domain-containing proteins is a conserved disulfide bond...

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Rok 2012

• Pilicides effectively hinder chaperone-usher interactions in all Gram-negative bacteria

  Publikacja

  • J. Pilipczuk
  • B. Zalewska-Piątek
  • K. Dzierzbicka
  • S. Makowiec
  • R. Piątek
  • A. Cyrancka-Czaja

  - Rok 2012

  The chaperone-usher pathway of adhesive structures biogenesis is highly conserved in all Gram-negative bacteria. Pili are polymers of thousands protein subunits that possess conserved immunoglobuline-like structure denoted by lack of the seventh G strand. The effect of this structural defect is a hydrophobic acceptor cleft. The folding of protein subunits is strictly dependent on the action of specific periplasmic chaperone protein...

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