FpvA bound to non-cognate pyoverdines: molecular basis of siderophore recognition by an iron transporter

Autor: Franc Pattus, Valérie A. Geoffroy, Jason Greenwald, Mirella Nader, Christelle Gruffaz, Hervé Celia, Isabelle J. Schalk, Jean Marie Meyer
Přispěvatelé: Biotechnologie et signalisation cellulaire (BSC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Institut de recherche de l'Ecole de biotechnologie de Strasbourg (IREBS), Institut Gilbert-Laustriat : Biomolécules, Biotechnologie, Innovation Thérapeutique, Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS), Génétique moléculaire, génomique, microbiologie (GMGM), Centre National de la Recherche Scientifique (CNRS), Université Louis Pasteur - Strasbourg I, Celia, Herve
Jazyk: angličtina
Rok vydání: 2009
Předmět:
Siderophore
Iron
Siderophores
Plasma protein binding
Biology
Ligands
Microbiology
FpvA
Substrate Specificity
03 medical and health sciences
chemistry.chemical_compound
Protein structure
medicine
[SDV.BBM] Life Sciences [q-bio]/Biochemistry
Molecular Biology
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
Binding site
Molecular Biology
030304 developmental biology
0303 health sciences
Pyoverdine
030306 microbiology
pyoverdine
Circular Dichroism
Transporter
Gene Expression Regulation
Bacterial
biology.organism_classification
Sciences du Vivant [q-bio]/Microbiologie et Parasitologie
Protein Structure
Tertiary
[SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology
chemistry
Biochemistry
Pseudomonas aeruginosa
Ferric
Oligopeptides
Bacteria
medicine.drug
Bacterial Outer Membrane Proteins
Protein Binding
Zdroj: Molecular Microbiology
Molecular Microbiology, Wiley, 2009, 72 (5), pp.1246-1259. ⟨10.1111/j.1365-2958.2009.06721.x⟩
Molecular Microbiology, Wiley, 2009, 72 (5), pp.1246-59
ISSN: 0950-382X
1365-2958
DOI: 10.1111/j.1365-2958.2009.06721.x⟩
Popis: International audience; The first step in the specific uptake of iron via siderophores in Gram-negative bacteria is the recognition and binding of a ferric siderophore by its cognate receptor. We investigated the molecular basis of this event through structural and biochemical approaches. FpvA, the pyoverdine-Fe transporter from Pseudomonas aeruginosa ATCC 15692 (PAO1 strain), is able to transport ferric-pyoverdines originating from other species, whereas most fluorescent pseudomonads are only able to use the one they produce among the more than 100 known different pyoverdines. We solved the structure of FpvA bound to non-cognate pyoverdines of high- or low-affinity and found a close correlation between receptor-ligand structure and the measured affinities. The structure of the first amino acid residues of the pyoverdine chain distinguished the high- and low-affinity binders while the C-terminal portion of the pyoverdines, often cyclic, does not appear to contribute extensively to the interaction between the siderophore and its transporter. The specificity of the ferric-pyoverdine binding site of FpvA is conferred by the structural elements common to all ferric-pyoverdines, i.e. the chromophore, iron, and its chelating groups.
Databáze: OpenAIRE
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