1EFD

PERIPLASMIC FERRIC SIDEROPHORE BINDING PROTEIN FHUD COMPLEXED WITH GALLICHROME

Summary for 1EFD

• Entry DOI: 10.2210/pdb1efd/pdb
• Descriptor: FERRICHROME-BINDING PERIPLASMIC PROTEIN, GALLICHROME (3 entities in total)
• Functional Keywords: periplasmic binding protein-siderophore complex, fhud complex with gallichrome, escherichia coli, ferric siderophore binding protein, metal transport
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 30464.60

Authors

Clarke, T.E.,Ku, S.-Y.,Dougan, D.R.,Vogel, H.J.,Tari, L.W. (deposition date: 2000-02-07, release date: 2000-04-05, Last modification date: 2024-02-07)

Primary citation

Clarke, T.E.,Ku, S.Y.,Dougan, D.R.,Vogel, H.J.,Tari, L.W.
The structure of the ferric siderophore binding protein FhuD complexed with gallichrome.
Nat.Struct.Biol., 7:287-291, 2000

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 ¿ 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.

PubMed: 10742172
DOI: 10.1038/74048

Experimental method

X-RAY DIFFRACTION (1.9 Å)