Porins are bacterial β-strand proteins that form a water-filled β-barrel pore within the outer membrane, either causing a disruption of the membrane or generating a means for transporting molecules such as carbohydrates and amino acids across the membrane. Porins allow for passive diffusion and so are considered membrane transport proteins and channels.

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    Cryo-EM, crystallography, biochemical experiments and computational approaches have been used to study different intermediate states of the Aeromonas hydrophila toxin aerolysin en route to pore formation. These results reveal that an unexpected and marked rotation of the core aerolysin machinery is required to unleash the membrane-spanning regions.

    • James C Whisstock
    •  & Michelle A Dunstone