6E4V
The Crystal Structure of FhuE from E. coli in complex with its substrate Coprogen
Summary for 6E4V
| Entry DOI | 10.2210/pdb6e4v/pdb |
| Descriptor | FhuE receptor, octyl beta-D-glucopyranoside, COPROGEN, ... (4 entities in total) |
| Functional Keywords | tonb-dependent transporter, coprogen, gram-negative bacteria, outer membrane, iron transport, transport protein |
| Biological source | Escherichia coli BW25113 |
| Total number of polymer chains | 1 |
| Total formula weight | 79757.26 |
| Authors | Grinter, R.,Lithgow, T. (deposition date: 2018-07-18, release date: 2019-04-10, Last modification date: 2023-10-11) |
| Primary citation | Grinter, R.,Lithgow, T. Determination of the molecular basis for coprogen import by Gram-negative bacteria. Iucrj, 6:401-411, 2019 Cited by PubMed Abstract: In order to survive in mixed microbial communities, some species of fungi secrete coprogens, siderophores that facilitate capture of the scarce nutrient iron. The TonB-dependent transporter FhuE is integrated in the outer membrane of Gram-negative bacteria and has been reported to scavenge these fungally produced coprogens. In this work, an strain was engineered that is dependent solely on FhuE for its access to siderophore-sequestered iron. Using this tool, it is shown that while FhuE is highly active in the import of coprogens, it has some level of promiscuity, acting as a low-affinity transporter for related siderophores. The crystal structure of FhuE in complex with coprogen was determined, providing a structural basis to explain this selective promiscuity. The structural data, in combination with functional analysis, presented in this work show that FhuE has evolved to specifically engage with planar siderophores. A potential evolutionary driver, and a critical consequence of this selectivity, is that it allows FhuE to exclude antibiotics that mimic nonplanar hydroxamate siderophores: these toxic molecules could otherwise cross the outer membrane barrier through a Trojan horse mechanism. PubMed: 31098021DOI: 10.1107/S2052252519002926 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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