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Interactions between residues in staphylococcal alpha-hemolysin revealed by reversion mutagenesis.

Abstract:

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 mutagenesis. alpha HL-H35N, in which the histidine at position 35 of the wild-type sequence is replaced with asparagine, is nonlytic and is arrested in assembly as a heptameric prepore. In this stud...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.270.39.23072

Authors


Panchal, RG More by this author
Journal:
The Journal of biological chemistry
Volume:
270
Issue:
39
Pages:
23072-23076
Publication date:
1995-09-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:a35fc966-dbbd-43e2-a77a-feeb5db056b9
Source identifiers:
52275
Local pid:
pubs:52275

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