Structural highlights
Function
[FIU_ECOLI] Involved in the active transport across the outer membrane of iron complexed with catecholate siderophores such as dihydroxybenzoylserine and dihydroxybenzoate. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. Can also transport catechol-substituted cephalosporins. Receptor for microcins M, H47 and E492.[1] [2] [3] [4] [5]
References
- ↑ Patzer SI, Baquero MR, Bravo D, Moreno F, Hantke K. The colicin G, H and X determinants encode microcins M and H47, which might utilize the catecholate siderophore receptors FepA, Cir, Fiu and IroN. Microbiology. 2003 Sep;149(Pt 9):2557-70. doi: 10.1099/mic.0.26396-0. PMID:12949180 doi:http://dx.doi.org/10.1099/mic.0.26396-0
- ↑ Destoumieux-Garzon D, Peduzzi J, Thomas X, Djediat C, Rebuffat S. Parasitism of iron-siderophore receptors of Escherichia coli by the siderophore-peptide microcin E492m and its unmodified counterpart. Biometals. 2006 Apr;19(2):181-91. doi: 10.1007/s10534-005-4452-9. PMID:16718603 doi:http://dx.doi.org/10.1007/s10534-005-4452-9
- ↑ Hantke K. Dihydroxybenzoylserine--a siderophore for E. coli. FEMS Microbiol Lett. 1990 Jan 15;55(1-2):5-8. PMID:2139424
- ↑ Nikaido H, Rosenberg EY. Cir and Fiu proteins in the outer membrane of Escherichia coli catalyze transport of monomeric catechols: study with beta-lactam antibiotics containing catechol and analogous groups. J Bacteriol. 1990 Mar;172(3):1361-7. PMID:2407721
- ↑ Curtis NA, Eisenstadt RL, East SJ, Cornford RJ, Walker LA, White AJ. Iron-regulated outer membrane proteins of Escherichia coli K-12 and mechanism of action of catechol-substituted cephalosporins. Antimicrob Agents Chemother. 1988 Dec;32(12):1879-86. PMID:3072926
