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A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore.


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 "phi-clamp" structure was required for protein translocation and comprised the major conductance-blocking site for hydrophobic drugs and model cations. We conclude that the phi clamp serves a chaperone-like function, interacting with hydrophobic sequences presented by the protein substrate as it unfolds during translocation.

SUBMITTER: Krantz BA 

PROVIDER: S-EPMC1815389 | biostudies-literature | 2005 Jul

REPOSITORIES: biostudies-literature

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A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore.

Krantz Bryan A BA   Melnyk Roman A RA   Zhang Sen S   Juris Stephen J SJ   Lacy D Borden DB   Wu Zhengyan Z   Finkelstein Alan A   Collier R John RJ  

Science (New York, N.Y.) 20050701 5735


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 "phi-clamp" structure was required for protein translocation and comprised the major  ...[more]

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