β-barrel membrane protein folding and structure viewed through the lens of α-hemolysin

Michelle Montoya, Eric Gouaux

Research output: Contribution to journalReview article

88 Scopus citations

Abstract

The β-barrel is a transmembrane structural motif commonly encountered in bacterial outer membrane proteins and pore-forming toxins (PFTs). α-Hemolysin (αHL) is a cytotoxin secreted by Staphylococcus aureus that assembles from a water-soluble monomer to form a membrane-bound heptameric β-barrel on the surface of susceptible cells, perforating the cell membranes, leading to cell death and lysis. The mechanism of heptamer assembly, which has been studied extensively, occurs in a stepwise manner, and the structures of the initial, monomeric form and final, membrane-embedded pore are known. The toxin's ability to assemble from an aqueous, hydrophilic species to a membrane-inserted oligomer is of interest in understanding the assembly of PFTs in particular and the folding and structure of β-barrel membrane proteins in general. Here we review the structures of the monomeric and heptamer states of LukF and αHL, respectively, the mechanism of toxin assembly, and the relationships between αHL and nontoxin β-barrel membrane proteins.

Original languageEnglish (US)
Pages (from-to)19-27
Number of pages9
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1609
Issue number1
DOIs
StatePublished - Jan 10 2003

Keywords

  • Protein folding
  • α-Hemolysin
  • β-Barrel

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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