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 Bioljournal_title
Current opinion in structural biologyauthors
Tilley SJ,Saibil HRdoi
10.1016/j.sbi.2006.03.008subject
Has Abstractpub_date
2006-04-01 00:00:00pages
230-6issue
2eissn
0959-440Xissn
1879-033Xpii
S0959-440X(06)00046-7journal_volume
16pub_type
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