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- W2161696543 abstract "Staphylococcal leukocidin pores are formed by the obligatory interaction of two distinct polypeptides, one of class F and one of class S, making them unique in the family of beta-barrel pore-forming toxins (beta-PFTs). By contrast, other beta-PFTs form homo-oligomeric pores; for example, the staphylococcal alpha-hemolysin (alpha HL) pore is a homoheptamer. Here, we deduce the subunit composition of a leukocidin pore by two independent methods: gel shift electrophoresis and site-specific chemical modification during single-channel recording. Four LukF and four LukS subunits coassemble to form an octamer. This result in part explains properties of the leukocidin pore, such as its high conductance compared to the alpha HL pore. It is also pertinent to the mechanism of assembly of beta-PFT pores and suggests new possibilities for engineering these proteins." @default.
- W2161696543 created "2016-06-24" @default.
- W2161696543 creator A5068926322 @default.
- W2161696543 date "2002-04-01" @default.
- W2161696543 modified "2023-10-09" @default.
- W2161696543 title "Subunit composition of a bicomponent toxin: Staphylococcal leukocidin forms an octameric transmembrane pore" @default.
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- W2161696543 doi "https://doi.org/10.1110/ps.4360102" @default.
- W2161696543 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2373538" @default.
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- W2161696543 hasPublicationYear "2002" @default.
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