Formation of a gated channel by a ligand-specffic transport protein in the bacterial outer membrane

Jeanette M. Rutz, Jun Liu, Jeri Ann Lyons, Joanne Goranson, Sandra K. Armstrong, Mark A. McIntosh, Jimmy B. Feix, Phillip E. Klebba

Research output: Contribution to journalArticle

141 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)471-475
Number of pages5
JournalScience
Volume258
Issue number5081
DOIs
StatePublished - 1992

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    Rutz, J. M., Liu, J., Lyons, J. A., Goranson, J., Armstrong, S. K., McIntosh, M. A., Feix, J. B., & Klebba, P. E. (1992). Formation of a gated channel by a ligand-specffic transport protein in the bacterial outer membrane. Science, 258(5081), 471-475. https://doi.org/10.1126/science.1411544