Structural characterization of the urease accessory protein UreF from Klebsiella pneumoniae

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.

Source: Acta Crystallographica Section F - January 31, 2022 Category: Biochemistry Authors: Liu, S. Wu, W. Zhao, Q. Liang, H. Che, S. Zhang, H. Liu, R. Zhang, Q. Bartlam, M. Tags: UreF crystal structure urease Klebsiella pneumoniae research communications Source Type: research