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

Greenwald, Jason; Nader, Mirella; Celia, Hervé; Gruffaz, Christelle; Geoffroy, Valérie; Meyer, Jean Marie; Schalk, Isabelle J.; Pattus, Franc

doi:10.1111/j.1365-2958.2009.06721.x

Cited by 61 publications

(78 citation statements)

References 53 publications

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“…These data suggest a complex mechanism for CuMbn recognition and binding, wherein MbnT binds only structurally similar substrates, and individual MbnTs may bind cognate CuMbns with higher affinity than nonnative CuMbns. Similar trends are observed for the ferric pyoverdine receptor FpvA from Pseudomonas aeruginosa ATCC 15692, which, unlike other Pseudomonas TBDTs, binds noncognate pyoverdines, albeit with different affinities (28).…”

Section: Gene Regulation Patterns Of Transport Proteins In Ms Trichosupporting

confidence: 62%

“…Likely candidates for CuMbn transport include TonB-dependent transporters (TBDTs), outer membrane receptors that interact with the inner membrane TonB complex to transport substrates (25,26), including siderophores, sugars, metal chelates, and large protein cofactors like cobalamin (27), all of which bind with relatively high affinity. TBDTs also exhibit substrate specificity, binding even very similar substrates with different affinities (28).…”

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confidence: 99%

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Methanobactin transport machinery

Dassama

Kenney

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Methanotrophic bacteria use methane, a potent greenhouse gas, as their primary source of carbon and energy. The first step in methane metabolism is its oxidation to methanol. In almost all methanotrophs, this chemically challenging reaction is catalyzed by particulate methane monooxygenase (pMMO), a copper-dependent integral membrane enzyme. Methanotrophs acquire copper (Cu) for pMMO by secreting a small ribosomally produced, posttranslationally modified natural product called methanobactin (Mbn). Mbn chelates Cu with high affinity, and the Cu-loaded form (CuMbn) is reinternalized into the cell via an active transport process. Bioinformatic and gene regulation studies suggest that two proteins might play a role in CuMbn handling: the TonB-dependent transporter MbnT and the periplasmic binding protein MbnE. Disruption of the gene that encodes MbnT abolishes CuMbn uptake, as reported previously, and expression of MbnT in Escherichia coli confers the ability to take up CuMbn. Biophysical studies of MbnT and MbnE reveal specific interactions with CuMbn, and a crystal structure of apo MbnE is consistent with MbnE's proposed role as a periplasmic CuMbn transporter. Notably, MbnT and MbnE exhibit different levels of discrimination between cognate and noncognate CuMbns. These findings provide evidence for CuMbn–protein interactions and begin to elucidate the molecular mechanisms of its recognition and transport.

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Section: Gene Regulation Patterns Of Transport Proteins In Ms Trichosupporting

confidence: 62%

mentioning

confidence: 99%

Methanobactin transport machinery

Dassama

Kenney

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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“…These amino acid residues primarily interact with the pyoverdine chromophore and the hydroxamate-containing amino acids of the peptide chain (15). The specificity of Fpvs in binding and transport of cognate pyoverdines is well established (9,15), but Fpvs can also function in the uptake of ferric complexes of heterologous pyoverdines having similar peptide chain sequences (15)(16)(17). For example, FpvAI can bind and take up ferric-pyoverdines produced by several Pseudomonas spp., albeit with varied affinities.…”

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confidence: 99%

“…For example, FpvAI can bind and take up ferric-pyoverdines produced by several Pseudomonas spp., albeit with varied affinities. The first three residues of the pyoverdine peptide chain are the most critical determinants of affinity, but other factors, such as isomerization of the amino acid residues, also play a role in binding and transport by FpvAI (15).…”

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Ferric-Pyoverdine Recognition by Fpv Outer Membrane Proteins of Pseudomonas protegens Pf-5

Hartney¹,

Mazurier²,

Girard³

et al. 2012

Journal of Bacteriology

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eThe soil bacterium Pseudomonas protegens Pf-5 (previously called P. fluorescens Pf-5) produces two siderophores, enantio-pyochelin and a compound in the large and diverse pyoverdine family. Using high-resolution mass spectroscopy, we determined the structure of the pyoverdine produced by Pf-5. In addition to producing its own siderophores, Pf-5 also utilizes ferric complexes of some pyoverdines produced by other strains of Pseudomonas spp. as sources of iron. Previously, phylogenetic analysis of the 45 TonB-dependent outer membrane proteins in Pf-5 indicated that six are in a well-supported clade with ferric-pyoverdine receptors (Fpvs) from other Pseudomonas spp. We used a combination of phylogenetics, bioinformatics, mutagenesis, pyoverdine structural determinations, and cross-feeding bioassays to assign specific ferric-pyoverdine substrates to each of the six Fpvs of Pf-5. We identified at least one ferric-pyoverdine that was taken up by each of the six Fpvs of Pf-5. Functional redundancy of the Pf-5 Fpvs was also apparent, with some ferric-pyoverdines taken up by all mutants with a single Fpv deletion but not by a mutant having deletions in two of the Fpv-encoding genes. Finally, we demonstrated that phylogenetically related Fpvs take up ferric complexes of structurally related pyoverdines, thereby establishing structure-function relationships that can be employed in the future to predict the pyoverdine substrates of Fpvs in other Pseudomonas spp.

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Metal Trafficking Via Siderophores in Gram‐Negative Bacteria

Cobessi

Schalk

2004

Handbook of Metalloproteins

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Iron is essential for life for practically all living organisms and plays a number of key roles in biology. However, under physiological conditions, iron forms highly insoluble ferric hydroxide complexes, which severely limits its bioavailability. To overcome the problem of iron inaccessibility, bacteria excrete high‐affinity iron‐chelators termed siderophores that are able to solubilize iron and deliver it into the cells. In gram‐negative bacteria, the uptake of ferrisiderophores always involves, at the level of the outer membrane, specific transporters of the family of the TonB‐dependent receptors. The energy required for this uptake is provided by the proton‐motive force of the inner membrane by means of an inner membrane complex comprising three proteins, TonB, ExbB, and ExbD. Structures of TonB‐dependent receptors have been solved in different conformations. They are all composed of a β‐barrel occluded by a globular domain. The binding site is highly specific for a single siderophore and is located in the lumen on the extracellular side of the barrel. Some TonB‐dependent receptors have an additional N‐terminal domain located in the periplasm. These receptors, in parallel to transport ferrisiderophores across the outer membrane, are involved in a signaling cascade regulating expression of genes involved in iron acquisition.

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

Cited by 61 publications

References 53 publications

Methanobactin transport machinery

Methanobactin transport machinery

Ferric-Pyoverdine Recognition by Fpv Outer Membrane Proteins of Pseudomonas protegens Pf-5

Metal Trafficking Via Siderophores in Gram‐Negative Bacteria

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