Structural characterization of the urease accessory protein UreF from Klebsiella pneumoniae.
Acta Crystallogr F Struct Biol Commun
; 78(Pt 2): 75-80, 2022 Feb 01.
Article
in En
| MEDLINE
| ID: mdl-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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacterial Proteins
/
Urease
/
Klebsiella pneumoniae
Type of study:
Prognostic_studies
Language:
En
Journal:
Acta Crystallogr F Struct Biol Commun
Year:
2022
Document type:
Article