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

Hugo Lebrette; Céline Brochier-Armanet; Barbara Zambelli; Hilde De Reuse; Elise Borezée-Durant; Stéfano Ciurli; Christine Cavazza

doi:10.1016/j.str.2014.07.012

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

Hugo Lebrette ¹ Céline Brochier-Armanet ² Barbara Zambelli ³ Hilde De Reuse ⁴ Elise Borezée-Durant ⁵ Stéfano Ciurli ^{3, *} Christine Cavazza ^{6, *}

* Auteur correspondant

1 IBS - UMR 5075 - Institut de biologie structurale

2 LBBE - Laboratoire de Biométrie et Biologie Evolutive

3 Laboratory of Bioinorganic Chemistry, Department of Pharmacy and Biotechnology, University of Bologna, Viale Giuseppe Fanin, 40, 40127 Bologna, Italy

4 Pathogenèse de Helicobacter

5 MICALIS - MICrobiologie de l'ALImentation au Service de la Santé humaine

6 LCBM - UMR 5249 - Laboratoire de Chimie et Biologie des Métaux

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.

Keywords : ESCHERICHIA-COLI ABC-TRANSPORTER VIBRIO-PARAHAEMOLYTICUS X-RAY CRYSTALLOGRAPHY HELICOBACTER-PYLORI CRYSTAL-STRUCTURES STAPHYLOCOCCUS-AUREUS PEPTIDE-BINDING UREASE ACTIVITY NIKA

Type de document :

Article dans une revue

Stucture(London, England : 1993), 2014, 22 (10), pp.1421-1432. <10.1016/j.str.2014.07.012>

Domaine :

Sciences du Vivant [q-bio] / Biochimie, Biologie Moléculaire

Sciences du Vivant [q-bio] / Biochimie, Biologie Moléculaire / Biologie structurale [q-bio.BM]

Sciences du Vivant [q-bio] / Microbiologie et Parasitologie / Bactériologie

Sciences du Vivant [q-bio] / Médecine humaine et pathologie

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https://hal.archives-ouvertes.fr/hal-01084825
Contributeur : Nathalie Gon <>
Soumis le : jeudi 20 novembre 2014 - 10:53:37
Dernière modification le : mercredi 4 janvier 2017 - 16:14:22

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

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

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