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• W1969795354 endingPage "475" @default.
• W1969795354 startingPage "471" @default.
• W1969795354 abstract "The ferric enterobactin receptor (FepA) is a high-affinity ligand-specific transport protein in the outer membrane of Gram-negative bacteria. Deletion of the cell-surface ligand-binding peptides of FepA generated mutant proteins that were incapable of high-affinity uptake but that instead formed nonspecific, passive channels in the outer membrane. Unlike native FepA, these pores acted independently of the accessory protein TonB, which suggests that FepA is a gated porin and that TonB acts as its gatekeeper by facilitating the entry of ligands into the FepA channel. The sequence homology among TonB-dependent proteins suggests that all ligand-specific outer membrane receptors may function by this gated-porin mechanism." @default.
• W1969795354 created "2016-06-24" @default.
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• W1969795354 date "1992-10-16" @default.
• W1969795354 modified "2023-09-23" @default.
• W1969795354 title "Formation of a Gated Channel by a Ligand-Specific Transport Protein in the Bacterial Outer Membrane" @default.
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• W1969795354 doi "https://doi.org/10.1126/science.1411544" @default.
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