6BPM
The crystal structure of the Ferric-Catecholate import receptor Fiu from K12 E. coli: Closed form (C21)
Summary for 6BPM
| Entry DOI | 10.2210/pdb6bpm/pdb |
| Descriptor | Catecholate siderophore receptor Fiu, (20S)-2,5,8,11,14,17-HEXAMETHYL-3,6,9,12,15,18-HEXAOXAHENICOSANE-1,20-DIOL, octyl beta-D-glucopyranoside, ... (4 entities in total) |
| Functional Keywords | ferric-catecholate, tonb-dependent receptor, membrane transport, antibiotic uptake, iron transporter, membrane protein |
| Biological source | Escherichia coli (strain K12) |
| Total number of polymer chains | 2 |
| Total formula weight | 159963.07 |
| Authors | Grinter, R. (deposition date: 2017-11-23, release date: 2018-11-28, Last modification date: 2024-11-06) |
| Primary citation | Grinter, R.,Lithgow, T. The structure of the bacterial iron-catecholate transporter Fiu suggests that it imports substrates via a two-step mechanism. J.Biol.Chem., 2019 Cited by PubMed Abstract: The ferric iron uptake (Fiu) transporter from functions in the transport of iron-catecholate complexes across the bacterial outer membrane, providing the bacterium with iron, which is essential for growth. Recently it has become clear that Fiu also represents a liability for because its activity allows import of antimicrobial compounds that mimic catecholate. This inadvertent import suggests the potential utility of antimicrobial catechol siderophore mimetics in managing bacterial infections. However, to fully exploit these compounds, a detailed understanding of the mechanism of transport through Fiu and related transporters is required. To address this question, we determined the crystal structure of Fiu at 2.1-2.9 Å and analyzed its function in Through analysis of the Fiuo crystal structure, in combination with docking and mutagenesis, we provide insight into how Fiu and related transporters bind catecholate in a surface-exposed cavity. Moreover, through determination of the structure of Fiu in multiple crystal states, we revealed the presence of a large, selectively gated cavity in the interior of this transporter. This chamber is large enough to accommodate the Fiu substrate and may allow import of substrates via a two-step mechanism. This would avoid channel formation through the transporter and inadvertent import of toxic molecules. As Fiu and its homologs are the targets of substrate-mimicking antibiotics, these results may assist in the development of these compounds. PubMed: 31712312DOI: 10.1074/jbc.RA119.011018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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