1. Promiscuous nickel import in human pathogens: structure, thermodynamics, and evolution of extracytoplasmic nickel-binding proteins.
- Author
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Lebrette H, Brochier-Armanet C, Zambelli B, de Reuse H, Borezée-Durant E, Ciurli S, and Cavazza C
- Subjects
- Amino Acid Motifs, Amino Acid Sequence, Bacterial Proteins metabolism, Binding Sites, Biological Transport, Brucella suis chemistry, Brucella suis pathogenicity, Campylobacter jejuni chemistry, Campylobacter jejuni pathogenicity, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Phylogeny, Protein Conformation, Thermodynamics, Yersinia pestis chemistry, Yersinia pestis pathogenicity, Bacterial Proteins chemistry, Carrier Proteins chemistry, Carrier Proteins metabolism, Evolution, Molecular, Nickel metabolism
- 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., (Copyright © 2014 Elsevier Ltd. All rights reserved.)
- Published
- 2014
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