(Q27637443)

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X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin

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X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin (English)

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Escherichia coli

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author name string

Teresa E Clarke

1

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Volkmar Braun

2

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Gunther Winkelmann

3

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Leslie W Tari

4

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Hans J Vogel

5

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language of work or name

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publication date

19 April 2002

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Journal of Biological Chemistry

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277

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16

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13966-72

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Structural biology of bacterial iron uptake systems

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Iron acquisition systems in the pathogenic Neisseria

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The solution conformations of ferrichrome and deferriferrichrome determined by 1H-NMR spectroscopy and computational modeling.

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Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide

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Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA

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

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Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes

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Iron chelators in medicine

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Studies and syntheses of siderophores, microbial iron chelators, and analogs as potential drug delivery agents

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Uptake and Conversion of the Antibiotic Albomycin by Escherichia coli K-12

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Highly efficient uptake of a rifamycin derivative via the FhuA-TonB-dependent uptake route in Escherichia coli

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In vivo reconstitution of an active siderophore transport system by a binding protein derivative lacking a signal sequence

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Processing of X-ray diffraction data collected in oscillation mode

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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PROCHECK: a program to check the stereochemical quality of protein structures

1 reference

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Stereochemical quality of protein structure coordinates

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Ferrichrome transport in Escherichia coli K-12: altered substrate specificity of mutated periplasmic FhuD and interaction of FhuD with the integral membrane protein FhuB.

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Rhodotorulic acid, a diketopiperazine dihydroxamic acid with growth-factor activity. I. Isolation and characterization

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Atomic structures of periplasmic binding proteins and the high-affinity active transport systems in bacteria.

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Crystal structure of the outer membrane active transporter FepA from Escherichia coli

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SETOR: hardware-lighted three-dimensional solid model representations of macromolecules

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Transmembrane Signaling across the Ligand-Gated FhuA Receptor

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Solution conformation of ferrichrome, a microbial iron transport cyclohexapeptide, as deduced by high resolution proton magnetic resonance

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21 January 2018

Identifiers

10.1074/JBC.M109385200

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