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Protein Sci. 1997 Dec;6(12):2631-5.

alpha-Hemolysin, gamma-hemolysin, and leukocidin from Staphylococcus aureus: distant in sequence but similar in structure.

Author information

1
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032, USA. jeg52@columbia.edu

Abstract

alpha-Hemolysin from Staphylococcus aureus assembles from a water-soluble, monomeric species to a membrane-bound heptamer on the surface of target cells, creating water-filled channels that lead to cell death and lysis. Staphylococcus aureus also produces the gamma-hemolysin and leukocidin toxins, which function as two component toxins in the disruption and lysis of erythrocytes and leukocytes. Analysis of the aligned sequences of alpha-hemolysin, gamma-hemolysin, and leukocidin in the context of the alpha-hemolysin heptamer structure supports the conclusion that even though the level of sequence identity between alpha-hemolysin and the gamma-hemolysin and leukocidin toxins is in the so-called twilight zone, the three-dimensional structures of the protomers are probably conserved. By analogy with alpha-hemolysin, gamma-hemolysin and leukocidin may also form oligomeric, transmembrane channels in which an antiparallel beta-barrel constitutes the primary membrane-embedded domain.

PMID:
9416613
PMCID:
PMC2143621
DOI:
10.1002/pro.5560061216
[Indexed for MEDLINE]
Free PMC Article

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