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Advances in cryoEM and its impact on ?-pore forming proteins.

ABSTRACT: Deployed by both hosts and pathogens, ?-pore-forming proteins (?-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 ?-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.

SUBMITTER: Boyd CM

PROVIDER: S-EPMC6302071 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature

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Advances in cryoEM and its impact on β-pore forming proteins.

Boyd Courtney M CM Bubeck Doryen D

Current opinion in structural biology 20180817

Deployed by both hosts and pathogens, β-pore-forming proteins (β-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 β-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. ...[more]

PMID: 30125772

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