Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 52, Issue -, Pages 41-49Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2018.07.010
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Funding
- CRUK Career Establishment Award [C26409/A16099]
- BBSRC Doctoral Training Program grant [BB/J014575/1]
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Deployed by both hosts and pathogens, beta-pore-forming proteins (beta-PFPs) rupture membranes and lyse target cells. Soluble protein monomers oligomerize on the lipid bilayer where they undergo dramatic structural rearrangements, resulting in a transmembrane beta-barrel pore. Advances in electron cryo-microscopy (cryoEM) sample preparation, image detection, and computational algorithms have led to a number of recent structures that reveal a molecular mechanism of pore formation in atomic detail.
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