Microbiology: A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore

Bryan A. Krantz, Roman A. Melnyk, Sen Zhang, Stephen J. Juris, D. Borden Lacy, Zhengyan Wu, Alan Finkelstein, R. John Collier

Research output: Contribution to journalArticle

217 Scopus citations

Abstract

The protective antigen component of anthrax toxin forms a homoheptameric pore in the endosomal membrane, creating a narrow passageway for the enzymatic components of the toxin to enter the cytosol. We found that, during conversion of the heptameric precursor to the pore, the seven phenylalanine-427 residues converged within the lumen, generating a radially symmetric heptad of solvent-exposed aromatic rings. This "φ-clamp" structure was required for protein translocation and comprised the major conductance-blocking site for hydrophobic drugs and model cations. We conclude that the φ clamp serves a chaperone-like function, interacting with hydrophobic sequences presented by the protein substrate as it unfolds during translocation.

Original languageEnglish (US)
Pages (from-to)777-781
Number of pages5
JournalScience
Volume309
Issue number5735
DOIs
StatePublished - Jul 29 2005

ASJC Scopus subject areas

  • General

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    Krantz, B. A., Melnyk, R. A., Zhang, S., Juris, S. J., Lacy, D. B., Wu, Z., Finkelstein, A., & Collier, R. J. (2005). Microbiology: A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore. Science, 309(5735), 777-781. https://doi.org/10.1126/science.1113380