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Journal article

Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification.

Abstract:

The alpha-hemolysin (alpha HL) polypeptide is secreted by Staphylococcus aureus as a water-soluble monomer that assembles into lipid bilayers to form cylindrical heptameric pores 1-2 nm in effective internal diameter. We have individually replaced each charged residue (79 of 293 amino acids) and four neutral residues in alpha HL with cysteine, which is not found in the wild-type protein. The properties of these mutants have been examined before and after modification with the 450-Da dianionic...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.270.39.23065

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Chemical Biology
Role:
Author
Journal:
The Journal of biological chemistry
Volume:
270
Issue:
39
Pages:
23065-23071
Publication date:
1995-09-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:b34767b1-9506-480a-8217-9eada6539db1
Source identifiers:
52274
Local pid:
pubs:52274

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