9ZLO

Crystal structure of Proteus mirabilis UreE

Summary for 9ZLO

• Entry DOI: 10.2210/pdb9zlo/pdb
• Descriptor: Urease accessory protein UreE (2 entities in total)
• Functional Keywords: nickel, metallochaperone, urease accessory protein, metal binding protein
• Biological source: Proteus mirabilis
• Total number of polymer chains: 2
• Total formula weight: 35832.61

Authors

Pan, J.,Mueller, S.L.,Furlong, E.J. (deposition date: 2025-12-09, release date: 2026-03-25)

Primary citation

Pan, J.,Mueller, S.L.,Tasneem, N.,Wu, Y.,Furlong, E.J.
Molecular structure and nickel-binding capacity of Proteus mirabilis UreE.
Acta Crystallogr D Struct Biol, 2026

PubMed Abstract: 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.

PubMed: 41834538
DOI: 10.1107/S2059798326001907

Experimental method

X-RAY DIFFRACTION (2 Å)