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

Nature Structural Biology volume 7, pages 287–291 (2000)Cite this article

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 Å 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.

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Figure 1: 2|Fo| - |Fc|αc electron density map at 1.9 Å resolution contoured at 1 σ around gallichrome and several proximal residues found in the binding pocket.
Figure 2: Overall structure of the FhuD–gallichrome complex.
Figure 3: Detailed view of gallichrome binding.
Figure 4: Overall charge of the FhuD–gallichrome complex.

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Acknowledgements

We would like to thank V. Braun (Universität Tübingen, Germany) and W. Köster (Zurich, Switzerland) for providing strains used in this study. We would also like to thank L. Howell and J. Berensden for generously providing access to beam time and L. Flaks at the X8C beamline at BNL for assistance with data collection. This work was supported by operating grants from the Alberta Heritage Foundation for Medical Research (AHFMR) and the University of Calgary to L.W.T. and a grant from the Medical Research Council of Canada to H.J.V. T.E.C. is a holder of an MRC Doctoral Research Award. S.-Y.K. was supported by a Natural Sciences and Engineering Research Council of Canada summer studentship. L.W.T. and H.J.V. hold Medical Scholar and Scientist Awards, respectively, from AHFMR.

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  1. Department of Biological Sciences, University of Calgary, 2500 University Drive N.W., T2N 1N4, Calgary, Alberta, Canada

    Teresa E. Clarke, Shao-Yang Ku, Douglas R. Dougan, Hans J. Vogel & Leslie W. Tari

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  1. Teresa E. Clarke
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Correspondence to Hans J. Vogel or Leslie W. Tari.

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Clarke, T., Ku, SY., Dougan, D. et al. The structure of the ferric siderophore binding protein FhuD complexed with gallichrome. Nat Struct Mol Biol 7, 287–291 (2000). https://doi.org/10.1038/74048

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