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The Maturation Pathway of Nickel Urease

School of Life Sciences, Centre for Protein Science and Crystallography, State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Hong Kong 999077, China
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Inorganics 2019, 7(7), 85; https://doi.org/10.3390/inorganics7070085
Received: 7 June 2019 / Revised: 28 June 2019 / Accepted: 4 July 2019 / Published: 6 July 2019
(This article belongs to the Special Issue Bioinorganic Chemistry of Nickel)
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Abstract

Maturation of urease involves post-translational insertion of nickel ions to form an active site with a carbamylated lysine ligand and is assisted by urease accessory proteins UreD, UreE, UreF and UreG. Here, we review our current understandings on how these urease accessory proteins facilitate the urease maturation. The urease maturation pathway involves the transfer of Ni2+ from UreE → UreG → UreF/UreD → urease. To avoid the release of the toxic metal to the cytoplasm, Ni2+ is transferred from one urease accessory protein to another through specific protein–protein interactions. One central theme depicts the role of guanosine triphosphate (GTP) binding/hydrolysis in regulating the binding/release of nickel ions and the formation of the protein complexes. The urease and [NiFe]-hydrogenase maturation pathways cross-talk with each other as UreE receives Ni2+ from hydrogenase maturation factor HypA. Finally, the druggability of the urease maturation pathway is reviewed. View Full-Text
Keywords: urease maturation; metallochaperone; nickel; G-protein; conformational change urease maturation; metallochaperone; nickel; G-protein; conformational change
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Nim, Y.S.; Wong, K.-B. The Maturation Pathway of Nickel Urease. Inorganics 2019, 7, 85.

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