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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5735
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pubmed:dateCreated |
2005-7-29
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipid Bilayers,
http://linkedlifedata.com/resource/pubmed/chemical/Onium Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Organophosphorus Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylalanine,
http://linkedlifedata.com/resource/pubmed/chemical/Quaternary Ammonium Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/anthrax toxin,
http://linkedlifedata.com/resource/pubmed/chemical/tetrabutylammonium,
http://linkedlifedata.com/resource/pubmed/chemical/tetraphenylphosphonium
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
29
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pubmed:volume |
309
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
777-81
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pubmed:dateRevised |
2011-2-15
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pubmed:meshHeading |
pubmed-meshheading:16051798-Amino Acid Sequence,
pubmed-meshheading:16051798-Amino Acid Substitution,
pubmed-meshheading:16051798-Antigens, Bacterial,
pubmed-meshheading:16051798-Bacillus anthracis,
pubmed-meshheading:16051798-Bacterial Toxins,
pubmed-meshheading:16051798-Binding Sites,
pubmed-meshheading:16051798-Cell Membrane,
pubmed-meshheading:16051798-Cytosol,
pubmed-meshheading:16051798-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:16051798-Endosomes,
pubmed-meshheading:16051798-Hydrogen-Ion Concentration,
pubmed-meshheading:16051798-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:16051798-Lipid Bilayers,
pubmed-meshheading:16051798-Models, Biological,
pubmed-meshheading:16051798-Models, Molecular,
pubmed-meshheading:16051798-Molecular Sequence Data,
pubmed-meshheading:16051798-Mutagenesis,
pubmed-meshheading:16051798-Onium Compounds,
pubmed-meshheading:16051798-Organophosphorus Compounds,
pubmed-meshheading:16051798-Phenylalanine,
pubmed-meshheading:16051798-Protein Conformation,
pubmed-meshheading:16051798-Protein Folding,
pubmed-meshheading:16051798-Quaternary Ammonium Compounds
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pubmed:year |
2005
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pubmed:articleTitle |
A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore.
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pubmed:affiliation |
Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, N.I.H., Extramural
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