The mechanism of pore formation by bacterial toxins.
A remarkable group of proteins challenge the notions that protein sequence determines a unique three-dimensional structure, and that membrane and soluble proteins are very distinct. The pore-forming toxins typically transform from soluble, monomeric proteins to oligomers that form transmembrane channels. Recent structural studies provide ideas about how these changes take place. The recently solved structures of the beta-pore-forming toxins LukS, epsilon-toxin and intermedilysin confirm that the pore-forming regions are initially folded up on the surfaces of the soluble precursors. To create the transmembrane pores, these regions must extend and refold into membrane-inserted beta-barrels.
Tilley
Sarah J
SJ
School of Crystallography, Birkbeck College, Malet Street, London WC1E 7HX, UK.
Saibil
Helen R
HR
D001427:Bacterial Toxins / Q000737:chemistry / Q000378:metabolism*; D003603:Cytotoxins / Q000737:chemistry / Q000502:physiology*; D008051:Lipid Bilayers / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding
D001427:Bacterial Toxins; D003603:Cytotoxins; D008051:Lipid Bilayers