title: Nickel recognition by bacterial importer proteins.
abstract: Nickel supports the growth of microbes from a variety of very different growth environments that affect nickel speciation. The mechanisms of nickel uptake and the molecular bases for the selectivity of this process are emerging. The recent surge of Ni-importer protein structures provides an understanding of Ni-recognition in the initial binding step of the import process. This review compares the structural basis for Ni-recognition in the complexes (ABC and ECF-type) that dominate primary (ATP-dependent) transport, with a focus on how the structures suggest mechanisms for Ni selectivity. The structures raise key questions about the mechanisms of nickel-transfer reactions involved in import. There is also a discussion of key experimental approaches necessary to help establish the physiological importance of these structures.
authors.affiliation: Department of Chemistry and School of Biological and Biomedical Sciences, Durham University, Durham, UK. peter.chivers@durham.ac.uk.
authors.forename: Peter T
authors.initials: PT
authors.lastname: Chivers
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry; D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D001692:Biological Transport; D016123:Campylobacter jejuni / Q000378:metabolism; D003600:Cytosol / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D016480:Helicobacter pylori / Q000378:metabolism; D008958:Models, Molecular; D008968:Molecular Conformation; D009532:Nickel / Q000737:chemistry*; D021381:Protein Transport; D013211:Staphylococcus aureus / Q000378:metabolism; D015010:Yersinia pestis / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D009532:Nickel; D000255:Adenosine Triphosphate