Formation of a gated channel by a ligand-specific transport protein in the bacterial outer membrane.
Formation of a gated channel by a ligand-specific transport protein in the bacterial outer membrane.
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细菌外膜中配体特异性转运蛋白形成门控通道。
DOI：
10.1126/science.1411544
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发表时间：
1992
期刊：
影响因子：
--
通讯作者：
Klebba,PE
中科院分区：
文献类型：
--
作者：
Rutz,JM;Liu,J;Lyons,JA;Goranson,J;Armstrong,SK;McIntosh,MA;Feix,JB;Klebba,PE
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.
