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Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore.

Abstract:

Elucidation of the accurate subunit stoichiometry of oligomeric membrane proteins is fraught with complexities. The interpretations of chemical cross-linking, analytical ultracentrifugation, gel filtration, and low-resolution electron microscopy studies are often ambiguous. Staphylococcal alpha-hemolysin (alpha HL), a homooligomeric toxin that forms channels in cell membranes, was believed to possess six subunits arranged around a sixfold axis of symmetry. Here, we report that analysis of x-r...

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Publication status:
Published

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Publisher copy:
10.1073/pnas.91.26.12828

Authors


Gouaux, JE More by this author
Hobaugh, MR More by this author
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Journal:
Proceedings of the National Academy of Sciences of the United States of America
Volume:
91
Issue:
26
Pages:
12828-12831
Publication date:
1994-12-05
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
URN:
uuid:d0847fbb-c9e6-441a-b5c3-eb734c75ef22
Source identifiers:
52441
Local pid:
pubs:52441

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