Abstract:We describe the cryo-EM structure of Clostridium perfringens β-toxin (CBP) in styrene maleic acid (SMA) discs, which represents the membrane-inserted pore form, at near atomic resolution. We show that CPB forms an octamer, which though having a similar conformation to the hetero-oligomeric pores of bicomponent leukocidins, features a different receptor binding region and a novel N-terminal β-barrel. The latter contains an additional selectivity filter and creates a bipolar pore. We propose that the N-terminal … Show more
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