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Promiscuous Nickel Import in Human Pathogens: Structure, Thermodynamics, and Evolution of Extracytoplasmic Nickel-Binding Proteins

Abstract : In human pathogenic bacteria, nickel is required for the activation of two enzymes, urease and [NiFe]-hydrogenase, necessary for host infection. Acquisition of Ni(II) is mediated by either permeases or ABC-importers, the latter including a subclass that involves an extracytoplasmic nickel-binding protein, Ni-BP. This study reports on the structure of three Ni-BPs from a diversity of human pathogens and on the existence of three new nickel-binding motifs. These are different from that previously described for Escherichia coli Ni-BP NikA, known to bind nickel via a nickelophore, and indicate a variegated ligand selectivity for Ni-BPs. The structures are consistent with ligand affinities measured in solution by calorimetry and challenge the hypothesis of a general requirement of nickelophores for nickel uptake by canonical ABC importers. Phylogenetic analyses showed that Ni-BPs have different evolutionary origins and emerged independently from peptide-binding proteins, possibly explaining the promiscuous behavior of this class of Ni(II) carriers.
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https://hal.archives-ouvertes.fr/hal-01084825
Contributor : Nathalie GON Connect in order to contact the contributor
Submitted on : Thursday, November 20, 2014 - 10:53:37 AM
Last modification on : Tuesday, October 18, 2022 - 4:20:50 AM

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Hugo Lebrette, Céline Brochier-Armanet, Barbara Zambelli, Hilde de Reuse, Elise Borezée-Durant, et al.. Promiscuous Nickel Import in Human Pathogens: Structure, Thermodynamics, and Evolution of Extracytoplasmic Nickel-Binding Proteins. Structure, 2014, 22 (10), pp.1421-1432. ⟨10.1016/j.str.2014.07.012⟩. ⟨hal-01084825⟩

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