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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.
AuthorsHugo Lebrette, Céline Brochier-Armanet, Barbara Zambelli, Hilde de Reuse, Elise Borezée-Durant, Stefano Ciurli, Christine Cavazza
JournalStructure (London, England : 1993) (Structure) Vol. 22 Issue 10 Pg. 1421-32 (Oct 07 2014) ISSN: 1878-4186 [Electronic] United States
PMID25199691 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
CopyrightCopyright © 2014 Elsevier Ltd. All rights reserved.
Chemical References
  • Bacterial Proteins
  • Carrier Proteins
  • Nickel
Topics
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Bacterial Proteins (chemistry, metabolism)
  • Binding Sites
  • Biological Transport
  • Brucella suis (chemistry, pathogenicity)
  • Campylobacter jejuni (chemistry, pathogenicity)
  • Carrier Proteins (chemistry, metabolism)
  • Crystallography, X-Ray
  • Evolution, Molecular
  • Models, Molecular
  • Molecular Sequence Data
  • Nickel (metabolism)
  • Phylogeny
  • Protein Conformation
  • Thermodynamics
  • Yersinia pestis (chemistry, pathogenicity)

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