6JC4

Crystal structure of the urease accessory protein UreF from Klebsiella pneumoniae

Summary for 6JC4

• Entry DOI: 10.2210/pdb6jc4/pdb
• Descriptor: Urease accessory protein UreF (2 entities in total)
• Functional Keywords: nickel-binding; urease accessory protein, metal binding protein
• Biological source: Klebsiella pneumoniae
• Total number of polymer chains: 4
• Total formula weight: 114848.05

Authors

Wu, W.,Zhang, Q.,Bartlam, M. (deposition date: 2019-01-28, release date: 2020-01-29, Last modification date: 2024-05-29)

Primary citation

Liu, S.,Wu, W.,Zhao, Q.,Liang, H.,Che, S.,Zhang, H.,Liu, R.,Zhang, Q.,Bartlam, M.
Structural characterization of the urease accessory protein UreF from Klebsiella pneumoniae.
Acta Crystallogr.,Sect.F, 78:75-80, 2022

PubMed 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 Ni 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.

PubMed: 35102896
DOI: 10.1107/S2053230X22000474

Experimental method

X-RAY DIFFRACTION (2.3 Å)