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| Goñi,F.M.; Ostolaza,H.. |
| Alpha-Hemolysin is synthesized as a 1024-amino acid polypeptide, then intracellularly activated by specific fatty acylation. A second activation step takes place in the extracellular medium through binding of Ca2+ ions. Even in the absence of fatty acids and Ca2+ HlyA is an amphipathic protein, with a tendency to self-aggregation. However, Ca2+-binding appears to expose hydrophobic patches on the protein surface, facilitating both self-aggregation and irreversible insertion into membranes. The protein may somehow bind membranes in the absence of divalent cations, but only when Ca2+ (or Sr2+, or Ba2+) is bound to the toxin in aqueous suspensions, i.e., prior to its interaction with bilayers, can <FONT FACE="Symbol">a</FONT>-hemolysin bind... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Alpha-hemolysin; Bacterial toxins; RTX toxins; Lipid-protein interactions; Calcium-binding proteins; Model membranes. |
| Ano: 1998 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1998000800002 |
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