The structure of the ferric siderophore binding protein FhuD complexed with gallichrome.
Article Details
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Clarke TE, Ku SY, Dougan DR, Vogel HJ, Tari LW
The structure of the ferric siderophore binding protein FhuD complexed with gallichrome.
Nat Struct Biol. 2000 Apr;7(4):287-91.
- PubMed ID
- 10742172 [ View in PubMed]
- Abstract
Siderophore binding proteins play a key role in the uptake of iron in many gram-positive and gram-negative bacteria. FhuD is a soluble periplasmic binding protein that transports ferrichrome and other hydroxamate siderophores. The crystal structure of FhuD from Escherichia coli in complex with the ferrichrome homolog gallichrome has been determined at 1.9 inverted question mark resolution, the first structure of a periplasmic binding protein involved in the uptake of siderophores. Gallichrome is held in a shallow pocket lined with aromatic groups; Arg and Tyr side chains interact directly with the hydroxamate moieties of the siderophore. FhuD possesses a novel fold, suggesting that its mechanisms of ligand binding and release are different from other structurally characterized periplasmic ligand binding proteins.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Gallichrome Iron(3+)-hydroxamate-binding protein FhuD Protein Escherichia coli (strain K12) UnknownAntagonistDetails - Polypeptides
Name UniProt ID Iron(3+)-hydroxamate-binding protein FhuD P07822 Details