2026/03/10 by Jiayi Pan, Sarah L. Mueller, Nuren Tasneem +2 · 1 voice
Environmental Science · Materials Science · #Chromium effects and bioremediation #Enzyme Structure and Function #Microbial Applications in Construction Materials
paper · doi:10.1107/s2059798326001907
openalex publication_date 2026/03/10 · openalex created_date 2026/03/17 · openalex updated_date 2026/07/23
UreE is a nickel chaperone that is required for the safe and efficient delivery of nickel to the active site of the metalloenzyme urease, which is a key virulence factor of the urinary-tract pathogen Proteus mirabilis. We investigated the structural features of P. mirabilis UreE (PmUreE) using protein X-ray crystallography and its nickel-binding capacity by inductively coupled plasma mass spectrometry. Here, we report a 2.0 Å resolution crystal structure of homodimeric PmUreE and show that it has the capacity to bind five Ni(II) ions per dimer. Truncation of the histidine-rich C-terminus reduced the nickel-binding capacity by two Ni(II) ions per dimer, and comparison with homologous UreE structures allowed the assignment of putative nickel-binding sites within the PmUreE structure. These findings increase our understanding of how PmUreE binds nickel and ultimately prevents this toxic metal from causing significant cellular damage in P. mirabilis.