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Article

Structural basis for pore-forming mechanism of staphylococcal α-hemolysin.

Toxicon : official journal of the International Society on Toxinology - 15 Dec 2015

Sugawara Takaki, Yamashita Daichi, Kato Koji, Peng Zhao, Ueda Junki, Kaneko Jun, Kamio Yoshiyuki, Tanaka Yoshikazu, Yao Min

Abstract excerpt

Staphylococcal α-hemolysin (α-HL) is a β-barrel pore-forming toxin (PFT) expressed by Staphylococcus aureus. α-HL is secreted as a water-soluble monomeric protein, which binds to target membranes and forms membrane-inserted heptameric pores. To explore the pore-forming mechanism of α-HL in detail, we determined the crystal structure of the α-HL monomer and prepore using H35A mutant and W179A/R200A mutant,...

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Identifiers

PMID: 26428390
DOI: 10.1016/j.toxicon.2015.09.033

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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