Interactions of a Periplasmic Binding Protein with a Tetradentate Siderophore Mimic

Raines, Daniel J.; Moroz, Olga V.; Wilson, K.S.; Duhme‐Klair, Anne‐Kathrin

doi:10.1002/anie.201300751

Cited by 23 publications

(39 citation statements)

References 35 publications

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“…As expected, all three crystals were in space group P1 with three protein monomers per asymmetric unit, consistent with the apo-CeuE structure (PDB ID code 3ZKW) (27). Crystal I showed no additional electron density in the CeuE binding pockets, indicating that the 90-min soaking time was too short.…”

supporting

confidence: 82%

“…The site opposite the weaker catecholate donor (ortho position) is occupied by the oxygen donor of Tyr288, whereas that opposite the stronger oxygen donor (meta position) is occupied by the nitrogen donor of His227, consistent with their respective trans-influence (29). Although the observed Fe(III) binding mode is similar to that which we reported previously for the C2-symmetric siderophore mimic 4-LICAM 4− (PDB ID code 5A1J) (27), the diserine backbone of bisDHBS 5− plays a key role in determining the orientation of the unsymmetrical natural siderophore. In both chains A and B, the carboxylate group in the backbone of bisDHBS 5− provides an additional negative charge and accepts a hydrogen bond from Arg249 (Fig.…”

supporting

confidence: 82%

“…Our cocrystal structures revealed that CeuE interacts with the coordinatively saturated Fe(III) complex of the hexadentate mimic MECAM 6− through electrostatic interactions and hydrogen bonding, whereas it binds the coordinatively unsaturated complex of the tetradentate mimic 4-LICAM 4− by recruiting the side chains of two amino acid residues (His227 and Tyr288) to complete the coordination sphere of the Fe(III) center. We established that His227 and Tyr288 are conserved among a subset of related PBPs, including VctP from V. cholerae, and suggested that this subset of PBPs undergo similar structural changes to adapt to the binding of lower-denticity siderophores (27). The recent report that V. cholerae most efficiently uses trisDHBS 7− and bisDHBS 5− for the acquisition of Fe(III) provided a partial confirmation of this prediction (24).…”

mentioning

confidence: 55%

“…By using siderophore mimics, we previously demonstrated that CeuE can bind the Fe(III) complexes of both hexadentate and tetradentate catecholate ligands (26,27). Our cocrystal structures revealed that CeuE interacts with the coordinatively saturated Fe(III) complex of the hexadentate mimic MECAM 6− through electrostatic interactions and hydrogen bonding, whereas it binds the coordinatively unsaturated complex of the tetradentate mimic 4-LICAM 4− by recruiting the side chains of two amino acid residues (His227 and Tyr288) to complete the coordination sphere of the Fe(III) center.…”

mentioning

confidence: 99%

“…A previously reported total synthesis of enterobactin was adapted to synthesize H 5 -bisDHBS, with modifications aimed at simplifying the procedures (28). The Fe(III) complex of bisDHBS 5− was soaked into apo-CeuE crystals, grown as reported previously (27). Experimental details for the preparation of the Fe(III) complex of bisDHBS 5− , crystal growth conditions, data collection, and refinement are provided in Supporting Information.…”

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confidence: 99%

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Bacteria in an intense competition for iron: Key component of the Campylobacter jejuni iron uptake system scavenges enterobactin hydrolysis product

Raines

Moroz

Blagova

et al. 2016

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

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To acquire essential Fe(III), bacteria produce and secrete siderophores with high affinity and selectivity for Fe(III) to mediate its uptake into the cell. Here, we show that the periplasmic binding protein CeuE of Campylobacter jejuni, which was previously thought to bind the Fe(III) complex of the hexadentate siderophore enterobactin (Kd ∼ 0.4 ± 0.1 µM), preferentially binds the Fe(III) complex of the tetradentate enterobactin hydrolysis product bis(2,3-dihydroxybenzoyl-l-Ser) (H5-bisDHBS) (Kd = 10.1 ± 3.8 nM). The protein selects Λ-configured [Fe(bisDHBS)]2− from a pool of diastereomeric Fe(III)-bisDHBS species that includes complexes with metal-to-ligand ratios of 1:1 and 2:3. Cocrystal structures show that, in addition to electrostatic interactions and hydrogen bonding, [Fe(bisDHBS)]2− binds through coordination of His227 and Tyr288 to the iron center. Similar binding is observed for the Fe(III) complex of the bidentate hydrolysis product 2,3-dihydroxybenzoyl-l-Ser, [Fe(monoDHBS)2]3−. The mutation of His227 and Tyr288 to noncoordinating residues (H227L/Y288F) resulted in a substantial loss of affinity for [Fe(bisDHBS)]2− (Kd ∼ 0.5 ± 0.2 µM). These results suggest a previously unidentified role for CeuE within the Fe(III) uptake system of C. jejuni, provide a molecular-level understanding of the underlying binding pocket adaptations, and rationalize reports on the use of enterobactin hydrolysis products by C. jejuni, Vibrio cholerae, and other bacteria with homologous periplasmic binding proteins.

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confidence: 82%

supporting

confidence: 82%

mentioning

confidence: 55%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Bacteria in an intense competition for iron: Key component of the Campylobacter jejuni iron uptake system scavenges enterobactin hydrolysis product

Raines

Moroz

Blagova

et al. 2016

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

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Extracytoplasmic Nickel‐Binding Proteins

Cavazza

2016

Encyclopedia of Inorganic and Bioinorganic Chemistry

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In bacteria, nickel is required for the activation of at least nine enzymes. Among several nickel import systems dedicated to Ni(II) acquisition, canonical ABC‐type importers possess an extracytoplasmic nickel‐binding protein (or Ni‐BP) that serves as the initial receptor and the major determinant of the transporter specificity. Ni‐BPs evolved from peptide‐BPs from at least four independent evolutionary origins. Their evolutionary history is dominated by horizontal gene transfers among bacteria and Archaea, among Gram‐positive and Gram‐negative bacteria, and among organisms having different lifestyles. Phylogeny of Ni‐BPs explains the promiscuous behavior of this class of Ni(II) carriers. In the Ni‐BPs family, a diversity of nickel‐binding motifs was identified, precluding the determination of a common consensus nickel‐binding mode. Different strategies to bind Ni(II) in the protein cavity have been described. Ni‐BPs binds either free nickel ions or chelated Ni(II). Naked nickel binds to the protein via three histidine residues. In several Ni‐BPs, only one histidine residue is involved in direct nickel–protein contact and a chelator that binds to the protein via supramolecular interactions is required to complete the coordination sphere of the metal. In Staphylococcus aureus , Ni‐BPs do not possess any histidine in their nickel‐binding motifs and the nickel complex is stabilized in the binding pockets via salt bridges with arginines and interactions with aromatic residues. Depending on the growth conditions and nickel availability in the environment, the chelators are either available molecules in the environment such as L‐histidine or by‐products of the metabolism or putative endogenous biosynthetic nickelophores.

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Bacterial Siderophore‐Binding ProteinFepB

Krewulak

Vogel

2016

Encyclopedia of Inorganic and Bioinorganic Chemistry

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Many bacteria can produce and secrete ferric‐iron‐specific chelators, called siderophores, to remove bound ferric iron from host proteins. The catecholate‐type siderophore enterobactin is a high‐affinity siderophore that is used by many Gram‐negative and Gram‐positive bacteria to acquire iron. In Gram‐negative bacteria, the ferric‐enterobactin (Fep) uptake system includes the outer membrane receptor FepA, the periplasmic binding protein (PBP) FepB, and the cytoplasmic membrane ABC transporter FepDG and FepC. FepB is a PBP with a type III structure fold, which has two independently folded domains linked together by a long α‐helix. This article will provide a comprehensive look at the structural and functional aspects of the 34 kDa PBP FepB.

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Interactions of a Periplasmic Binding Protein with a Tetradentate Siderophore Mimic

Cited by 23 publications

References 35 publications

Bacteria in an intense competition for iron: Key component of the Campylobacter jejuni iron uptake system scavenges enterobactin hydrolysis product

Bacteria in an intense competition for iron: Key component of the Campylobacter jejuni iron uptake system scavenges enterobactin hydrolysis product

Extracytoplasmic Nickel‐Binding Proteins

Bacterial Siderophore‐Binding ProteinFepB

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