作者
Hugo Lebrette, Celine Brochier-Armanet, Barbara Zambelli, Hilde De Reuse, Elise Borezée-Durant, Stefano Ciurli, Christine Cavazza
发表日期
2014/10/7
期刊
Structure
卷号
22
期号
10
页码范围
1421-1432
出版商
Elsevier
简介
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 …
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H Lebrette, C Brochier-Armanet, B Zambelli… - Structure, 2014