Functional complementation of staphylococcal alpha-hemolysin fragments. Overlaps, nicks, and gaps in the glycine-rich loop.
نویسندگان
چکیده
منابع مشابه
Mechanism of Action of Staphylococcal Alpha-hemolysin. I. Some Factors Influencing the Measurement of Alpha-hemolysin.
Marucci, Americo A. (Upstate Medical Center, Syracuse, N.Y.). Mechanism of action of staphylococcal alpha-hemolysin. I. Some factors influencing the measurement of alpha-hemolysin. J. Bacteriol. 86:1182-1188. 1963.-A kinetic method for the accurate and reproducible measurement of the action of staphylococcal alpha-hemolysin on rabbit erythrocytes is described. The activity of the alpha-hemolysi...
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15 صفحه اولStaphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers.
Atomic force microscopy (AFM) was used to study the structure of the staphylococcal alpha-hemolysin (alpha HL) oligomer formed in supported phospholipid bilayers. In contrast to the recent X-ray crystallographic demonstration of a heptameric stoichiometry for the oligomer formed in deoxycholate (DOC) micelles, the high-resolution unprocessed AFM images unequivocally revealed a hexamer in these ...
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The antibacterial protein Colicin V (ColV) is secreted from gram-negative bacteria by a signal sequence-independent pathway. The proteins that mediate the export of ColV share sequence similarities with components from other signal sequence-independent export systems such as those for alpha-hemolysin (Hly) and Erwinia protease (Prt). We report here that the intact HlyBD export system can export...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1993
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)53531-6