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Article

Disulfide-bond scanning reveals assembly state and β-strand tilt angle of the PFO β-barrel.

Nature chemical biology - 1 Jun 2013

Sato Takehiro K, Tweten Rodney K, Johnson Arthur E

Abstract excerpt

Perfringolysin O (PFO), a bacterial cholesterol-dependent cytolysin, binds a mammalian cell membrane, oligomerizes into a circular prepore complex (PPC) and forms a 250-Å transmembrane β-barrel pore in the cell membrane. Each PFO monomer has two sets of three short α-helices that unfold and ultimately refold into two transmembrane β-hairpin (TMH) components of the membrane-embedded β-barrel. Interstrand...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 23563525
DOI: 10.1038/nchembio.1228
PMCID: PMC3661704

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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