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Journal article

Spontaneous oligomerization of a staphylococcal alpha-hemolysin conformationally constrained by removal of residues that form the transmembrane beta-barrel.

Abstract:

Staphylococcal alpha-hemolysin is a water soluble, monomeric, bacterial exotoxin, which forms heptameric pores in membranes. The rate determining step in assembly is the conversion of a heptameric prepore to the fully assembled pore in which the central glycine-rich domain of each subunit inserts into the membrane to form a 14 strand beta barrel. Barrel formation is accompanied by a conformational change in which each N terminus latches onto an adjacent subunit. In the monomer in solution, th...

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Publication status:
Published

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Publisher copy:
10.1093/protein/10.12.1433

Authors


Malghani, MS More by this author
Hobaugh, M More by this author
Gouaux, JE More by this author
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Journal:
Protein engineering
Volume:
10
Issue:
12
Pages:
1433-1443
Publication date:
1997-12-05
DOI:
EISSN:
1460-213X
ISSN:
0269-2139
URN:
uuid:62ba2a9b-22bc-46f8-a8ec-bd0bc6cb45de
Source identifiers:
52297
Local pid:
pubs:52297

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