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Science 16 October 1992:
Vol. 258. no. 5081, pp. 471 - 475
DOI: 10.1126/science.1411544
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Articles

Science, Vol 258, Issue 5081, 471-475
Copyright © 1992 by American Association for the Advancement of Science

articles

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

JM Rutz, J Liu, JA Lyons, J Goranson, SK Armstrong, MA McIntosh, JB Feix, and PE Klebba

Department of Microbiology, Medical College of Wisconsin, Milwaukee 53226.

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.


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