The beta-barrel domain of FhuADelta5-160 is sufficient for TonB-dependent FhuA activities of Escherichia coli
Author:
Publisher
Wiley
Subject
Molecular Biology,Microbiology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.1365-2958.1999.01546.x/fullpdf
Reference43 articles.
1. FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5.
2. Maltose/Maltodextrin System of Escherichia coli : Transport, Metabolism, and Regulation
3. Specific In Vivo Labeling of Cell Surface-Exposed Protein Loops: Reactive Cysteines in the Predicted Gating Loop Mark a Ferrichrome Binding Site and a Ligand-Induced Conformational Change of the Escherichia coli FhuA Protein
4. The proton motive force drives the outer membrane transport of cobalamin in Escherichia coli
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