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Your search keyword '"enterobactin or enterochelin"' showing total 2 results
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2 results on '"enterobactin or enterochelin"'

1. Parsing the functional specificity of Siderocalin/Lipocalin 2/NGAL for siderophores and related small-molecule ligands.

Author

Clifton, Matthew C, Rupert, Peter B, Hoette, Trisha M, Raymond, Kenneth N, Abergel, Rebecca J, and Strong, Roland K

Subjects
ABC, ATP‐binding cassette, AEB, aerobactin, AU, crystallographic asymmetric unit, Antimicrobial responses, BOCT, brain-type organic cation receptor, Bacterial substrate binding proteins, CAM, catechol, CMB, carboxymycobactin, DHBA, dihydroxybenzoic acid, ENT, enterobactin or enterochelin, FQ, fluorescence quenching, Ferric enterobactin/enterochelin, HOPO, hydroxypyridinone, NE, norepinephrine, NGAL, Neutrophil Gelatinase Associated Lipocalin, PBP, bacterial periplasmic binding protein, PCH, pyochelin, PDB, Research Collaboratory for Structural Biology Protein Databank, PVD, pyoverdine, SBP, bacterial membrane-associated, substrate-binding protein, SCH, schizokinen, Scn, Siderocalin, X-ray crystallography, c-di-GMP, cyclic diguanylate monophosphate, Infection, Inflammatory and immune system
Abstract

Siderocalin/Lipocalin 2/Neutrophil Gelatinase Associated Lipocalin/24p3 is an innate immune system protein with bacteriostatic activity, acting by tightly binding and sequestering diverse catecholate and mixed-type ferric siderophores from enteric bacteria and mycobacteria. Bacterial virulence achieved through siderophore modifications, or utilization of alternate siderophores, can be explained by evasion of Siderocalin binding. Siderocalin has also been implicated in a wide variety of disease processes, though often in seemingly contradictory ways, and has been proposed to bind to a broader array of ligands beyond siderophores. Using structural, directed mutational, and binding studies, we have sought to rigorously test, and fully elucidate, the Siderocalin recognition mechanism. Several proposed ligands fail to meet rigorous binding criteria, including the bacterial siderophore pyochelin, the iron-chelating catecholamine hormone norepinephrine, and the bacterial second messenger cyclic diguanylate monophosphate. While possessing a remarkably rigid structure, in principle simplifying analyses of ligand recognition, understanding Scn recognition is complicated by the observed conformational and stoichiometric plasticity, and instability, of its bona fide siderophore ligands. Since the role of Siderocalin at the early host/pathogen interface is to compete for bacterial ferric siderophores, we also analyzed how bacterial siderophore binding proteins and enzymes alternately recognize siderophores that efficiently bind to, or evade, Siderocalin sequestration - including determining the crystal structure of Bacillus cereus YfiY bound to schizokinen. These studies combine to refine the potential physiological functions of Siderocalin by defining its multiplexed recognition mechanism.

Published
2019

2. Parsing the functional specificity of Siderocalin/Lipocalin 2/NGAL for siderophores and related small-molecule ligands

Author

Trisha M. Hoette, Rebecca J. Abergel, Kenneth N. Raymond, Matthew C. Clifton, Peter B. Rupert, and Roland K. Strong

Subjects
Siderophore, HOPO, hydroxypyridinone, dihydroxybenzoic acid, substrate-binding protein, PBP, bacterial periplasmic binding protein, CMB, Lipocalin, AEB, PBP, DHBA, dihydroxybenzoic acid, Structural Biology, BOCT, brain-type organic cation receptor, aerobactin, Bacterial substrate binding proteins, NGAL, Neutrophil Gelatinase Associated Lipocalin, PVD, pyoverdine, NGAL, SBP, bacterial membrane-associated, substrate-binding protein, lcsh:QH301-705.5, Ferric enterobactin/enterochelin, bacterial membrane-associated, 0303 health sciences, CAM, pyoverdine, Chemistry, 030302 biochemistry & molecular biology, PCH, c-di-GMP, cyclic diguanylate monophosphate, Small molecule, FQ, fluorescence quenching, Transport protein, schizokinen, Biochemistry, HOPO, Infection, ABC, DHBA, PDB, Research Collaboratory for Structural Biology Protein Databank, NE, AU, crystallographic asymmetric unit, ENT, fluorescence quenching, Siderocalin, ABC, ATP‐binding cassette, brain-type organic cation receptor, DNA-binding protein, Article, norepinephrine, CMB, carboxymycobactin, FQ, 03 medical and health sciences, carboxymycobactin, CAM, catechol, c-di-GMP, cyclic diguanylate monophosphate, SBP, PCH, pyochelin, hydroxypyridinone, AEB, aerobactin, ComputingMethodologies_COMPUTERGRAPHICS, X-ray crystallography, 030304 developmental biology, crystallographic asymmetric unit, Innate immune system, Ligand, Inflammatory and immune system, enterobactin or enterochelin, Antimicrobial responses, catechol, SCH, bacterial periplasmic binding protein, PDB, Research Collaboratory for Structural Biology Protein Databank, pyochelin, PVD, Scn, ENT, enterobactin or enterochelin, lcsh:Biology (General), BOCT, Neutrophil Gelatinase Associated Lipocalin, AU, ATP‐binding cassette, SCH, schizokinen, Scn, Siderocalin, NE, norepinephrine
Abstract

Graphical abstract, Highlights • Ligand recognition by antibacterial Siderocalin controls the competition for iron during infection. • We determined nine crystal structures of Siderocalin mutants with ligands. • We determined three candidate ligands did not bind. • We determined the crystal structure of SBP YfiY. • Multiplexed specificity of Siderocalin was determined., Siderocalin/Lipocalin 2/Neutrophil Gelatinase Associated Lipocalin/24p3 is an innate immune system protein with bacteriostatic activity, acting by tightly binding and sequestering diverse catecholate and mixed-type ferric siderophores from enteric bacteria and mycobacteria. Bacterial virulence achieved through siderophore modifications, or utilization of alternate siderophores, can be explained by evasion of Siderocalin binding. Siderocalin has also been implicated in a wide variety of disease processes, though often in seemingly contradictory ways, and has been proposed to bind to a broader array of ligands beyond siderophores. Using structural, directed mutational, and binding studies, we have sought to rigorously test, and fully elucidate, the Siderocalin recognition mechanism. Several proposed ligands fail to meet rigorous binding criteria, including the bacterial siderophore pyochelin, the iron-chelating catecholamine hormone norepinephrine, and the bacterial second messenger cyclic diguanylate monophosphate. While possessing a remarkably rigid structure, in principle simplifying analyses of ligand recognition, understanding Scn recognition is complicated by the observed conformational and stoichiometric plasticity, and instability, of its bona fide siderophore ligands. Since the role of Siderocalin at the early host/pathogen interface is to compete for bacterial ferric siderophores, we also analyzed how bacterial siderophore binding proteins and enzymes alternately recognize siderophores that efficiently bind to, or evade, Siderocalin sequestration – including determining the crystal structure of Bacillus cereus YfiY bound to schizokinen. These studies combine to refine the potential physiological functions of Siderocalin by defining its multiplexed recognition mechanism.

Published
2019

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