Formation of a gated channel by a ligand-specific transport protein in the bacterial outer membrane. Science 1992 Oct 16;258(5081):471-5
Date
10/16/1992Pubmed ID
1411544DOI
10.1126/science.1411544Scopus ID
2-s2.0-0026545681 (requires institutional sign-in at Scopus site) 155 CitationsAbstract
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.
Author List
Rutz JM, Liu J, Lyons JA, Goranson J, Armstrong SK, McIntosh MA, Feix JB, Klebba PEAuthor
Jimmy B. Feix PhD Professor in the Biophysics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceAntigens, Bacterial
Antigens, Surface
Bacterial Outer Membrane Proteins
Carrier Proteins
DNA Mutational Analysis
Enterobactin
Escherichia coli
Ion Channel Gating
Microbial Sensitivity Tests
Molecular Sequence Data
Receptors, Cell Surface
Structure-Activity Relationship
