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...
Prif Awduron: | Panchal, R, Bayley, H |
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Fformat: | Journal article |
Iaith: | English |
Cyhoeddwyd: |
1995
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Eitemau Tebyg
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Assembly of the oligomeric membrane pore formed by Staphylococcal alpha-hemolysin examined by truncation mutagenesis.
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Cyhoeddwyd: (1992) -
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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Cyhoeddwyd: (1995) -
Surface labeling of key residues during assembly of the transmembrane pore formed by staphylococcal alpha-hemolysin.
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Cyhoeddwyd: (1994) -
The internal cavity of the staphylococcal alpha-hemolysin pore accommodates approximately 175 exogenous amino acid residues.
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Cyhoeddwyd: (2005) -
Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore.
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Cyhoeddwyd: (1996)