Structure and membrane topography of the vibrio-type secretin complex from the type 2 secretion system of enteropathogenic Escherichia coli

Iain D. Hay, Matthew J. Belousoff, Rhys A. Dunstan, Rebecca S. Bamert, Trevor Lithgow

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31 Citations (Scopus)


The β-barrel assembly machinery (BAM) complex is the core machinery for the assembly of β-barrel membrane proteins, and inhibition of BAM complex activity is lethal to bacteria. Discovery of integral membrane proteins that are key to pathogenesis and yet do not require assistance from the BAM complex raises the question of how these proteins assemble into bacterial outer membranes. Here, we address this question through a structural analysis of the type 2 secretion system (T2SS) secretin from enteropathogenic Escherichia coli O127:H6 strain E2348/69. Long β-strands assemble into a barrel extending 17 Å through and beyond the outer membrane, adding insight to how these extensive β-strands are assembled into the E. coli outer membrane. The substrate docking chamber of this secretin is shown to be sufficient to accommodate the substrate mucinase SteC.

Original languageEnglish
Article numbere00521-17
Number of pages15
JournalJournal of Bacteriology
Issue number5
Publication statusPublished - 1 Mar 2018


  • protein secretion
  • bacterial pathogenesis
  • BAM complex
  • transertion
  • outer membrane
  • lipoproteins
  • secretin

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