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  • Title: Structural characterization of the urease accessory protein UreF from Klebsiella pneumoniae.
    Author: Liu S, Wu W, Zhao Q, Liang H, Che S, Zhang H, Liu R, Zhang Q, Bartlam M.
    Journal: Acta Crystallogr F Struct Biol Commun; 2022 Feb 01; 78(Pt 2):75-80. PubMed ID: 35102896.
    Abstract:
    Klebsiella pneumoniae is an opportunistic pathogen that mostly affects those with weakened immune systems. Urease is a vital enzyme that can hydrolyze urea to ammonia and carbon dioxide as a source of nitrogen for growth. Urease is also a K. pneumoniae virulence factor that enables survival of the bacterium under nutrient-limiting conditions. UreF, an important nickel-binding urease accessory protein, is involved in the insertion of Ni2+ into the active site of urease. Here, the crystal structure of UreF from K. pneumoniae (KpUreF) is reported. Functional data show that KpUreF forms a stable dimer in solution. These results may provide a starting point for the design of urease inhibitors.
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