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 chan...

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Bibliographic Details
Published inCurrent opinion in structural biology Vol. 16; no. 2; pp. 230 - 236
Main Authors Tilley, Sarah J, Saibil, Helen R
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.04.2006
Subjects
Bacteria
Bacterial Toxins - chemistry
Bacterial Toxins - metabolism
Cytotoxins - chemistry
Cytotoxins - physiology
Lipid Bilayers - chemistry
Models, Molecular
Protein Conformation
Protein Folding
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Summary: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 β-pore-forming toxins LukS, ɛ-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 β-barrels.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
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ObjectType-Review-1
ISSN:0959-440X
1879-033X
DOI:10.1016/j.sbi.2006.03.008