The structure of the ferric siderophore binding protein FhuD complexed with gallichrome.

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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

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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)	Unknown	Antagonist	Details

Polypeptides

Name	UniProt ID
Iron(3+)-hydroxamate-binding protein FhuD	P07822	Details