Structural and mechanistic features of ClyA-like α-pore-forming toxins

Bastian Bräuning, Michael Groll

Research output: Contribution to journalReview articlepeer-review

11 Scopus citations

Abstract

Recent technological advances have seen increasing numbers of complex structures from diverse pore-forming toxins (PFT). The ClyA family of α-PFTs comprises a broad variety of assemblies including single-, two-and three-component toxin systems. With crystal structures available for soluble subunits of all major groups in this extended protein family, efforts now focus on obtaining molecular insights into physiological pore formation. This review provides an up-to-date discussion on common and divergent structural and functional traits that distinguish the various ClyA family PFTs. Open questions of this research topic are outlined and discussed.

Original languageEnglish
Article number343
JournalToxins
Volume10
Issue number9
DOIs
StatePublished - Sep 2018

Keywords

  • Cryo-electron microscopy
  • Pore-forming toxins (PFT)
  • Structural biology
  • Virulence factors
  • X-ray crystallography

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