The mechanism of pore formation by bacterial toxins.

Abstract:

: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.

journal_name

Curr Opin Struct Biol

authors

Tilley SJ,Saibil HR

doi

10.1016/j.sbi.2006.03.008

subject

Has Abstract

pub_date

2006-04-01 00:00:00

pages

230-6

issue

2

eissn

0959-440X

issn

1879-033X

pii

S0959-440X(06)00046-7

journal_volume

16

pub_type

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