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Mechanism of bacterial nickel import by Type I ABC transporters

Nickel is an essential cofactor for the function of at least nine fundamental bacterial enzyme families, including ureases, NiFe-hydrogenases and carbon monoxide dehydrogenases. In many bacteria, nickel import across the inner membrane is mediated by Type I ATP-binding cassette (ABC) transporter systems. These systems are composed of five proteins: one periplasmic nickel binding protein, heterodimeric transmembrane domains and heterodimeric nucleotide binding domains. Here we present cryogenic electron microscopy structures and crystal structures of components of the primary nickel importer system, Ynt, from the uropathogen Proteus mirabilis. Our analysis highlights conserved key residues for nickel transport and distinct roles of the transmembrane domains in the import cycle. Ultimately, revealing a mechanism for nickel transport across the bacterial inner membrane.

Dr Emily Furlong is an emerging leader in structural bacteriology whose research focuses on understanding the structure and function of novel antibacterial targets. She trained at the University of Queensland and University of Oxford, graduating with her PhD in 2019. She subsequently undertook postdoctoral research at Oxford and the Victor Chang Cardiac Research Institute in Sydney. In 2023, she established her research group at the Australian National University’s Research School of Biology, with the support of an ANU Futures Award.