Interactions between residues in staphylococcal alpha-hemolysin revealed by reversion mutagenesis.
alpha-Hemolysin (alpha HL), a pore-forming polypeptide of 293 amino acids, is secreted by Staphylococcus aureus as a water-soluble monomer. Residues that play key roles in the formation of functional heptameric pores on rabbit red blood cells (rRBC) have been identified previously by site-directed m...
Үндсэн зохиолчид: | Panchal, R, Bayley, H |
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Формат: | Journal article |
Хэл сонгох: | English |
Хэвлэсэн: |
1995
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Ижил төстэй зүйлс
Ижил төстэй зүйлс
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Assembly of the oligomeric membrane pore formed by Staphylococcal alpha-hemolysin examined by truncation mutagenesis.
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Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification.
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Surface labeling of key residues during assembly of the transmembrane pore formed by staphylococcal alpha-hemolysin.
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The internal cavity of the staphylococcal alpha-hemolysin pore accommodates approximately 175 exogenous amino acid residues.
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Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore.
-н: Song, L, зэрэг
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