5ADV

The Periplasmic Binding Protein CeuE of Campylobacter jejuni preferentially binds the iron(III) complex of the Linear Dimer Component of Enterobactin

Summary for 5ADV

• Entry DOI: 10.2210/pdb5adv/pdb
• Related: 5ADW
• Descriptor: ENTEROCHELIN UPTAKE PERIPLASMIC BINDING PROTEIN, FE (III) ION, 2-(2,3-DIHYDROXY-BENZOYLAMINO)-3-HYDROXY-PROPIONIC ACID, ... (6 entities in total)
• Functional Keywords: metal binding protein, enterobactin uptake, iron, siderophore, binding protein, tetradentate
• Biological source: CAMPYLOBACTER JEJUNI
• Total number of polymer chains: 3
• Total formula weight: 97007.76

Authors

Raines, D.J.,Moroz, O.V.,Turkenburg, J.P.,Wilson, K.S.,Duhme-Klair, A.K. (deposition date: 2015-08-24, release date: 2016-05-25, Last modification date: 2024-01-10)

Primary citation

Raines, D.J.,Moroz, O.V.,Blagova, E.V.,Turkenburg, J.P.,Wilson, K.S.,Duhme-Klair, A.
Bacteria in an Intense Competition for Iron: Key Component of the Campylobacter Jejuni Iron Uptake System Scavenges Enterobactin Hydrolysis Product.
Proc.Natl.Acad.Sci.USA, 113:5850-, 2016

PubMed Abstract: 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.

PubMed: 27162326
DOI: 10.1073/PNAS.1520829113

Experimental method

X-RAY DIFFRACTION (2.1 Å)