3TJ9

Crystal structure of Helicobacter pylori UreE bound to Zn2+

Summary for 3TJ9

• Entry DOI: 10.2210/pdb3tj9/pdb
• Related: 3TJ8 3TJA
• Descriptor: Urease accessory protein ureE, ZINC ION, FORMIC ACID, ... (4 entities in total)
• Functional Keywords: metal binding protein, urease accessory protein
• Biological source: Helicobacter pylori
• Cellular location: Cytoplasm: Q09064
• Total number of polymer chains: 4
• Total formula weight: 77927.03

Authors

Banaszak, K.,Bellucci, M.,Zambelli, B.,Rypniewski, W.R.,Ciurli, S. (deposition date: 2011-08-24, release date: 2011-11-02, Last modification date: 2024-02-28)

Primary citation

Banaszak, K.,Martin-Diaconescu, V.,Bellucci, M.,Zambelli, B.,Rypniewski, W.,Maroney, M.J.,Ciurli, S.
Crystallographic and X-ray absorption spectroscopic characterization of Helicobacter pylori UreE bound to Ni2+ and Zn2+ reveals a role for the disordered C-terminal arm in metal trafficking.
Biochem.J., 441:1017-1026, 2012

PubMed Abstract: The survival and growth of the pathogen Helicobacter pylori in the gastric acidic environment is ensured by the activity of urease, an enzyme containing two essential Ni²⁺ ions in the active site. The metallo-chaperone UreE facilitates in vivo Ni²⁺ insertion into the apoenzyme. Crystals of apo-HpUreE (H. pylori UreE) and its Ni⁺- and Zn⁺-bound forms were obtained from protein solutions in the absence and presence of the metal ions. The crystal structures of the homodimeric protein, determined at 2.00 Å (apo), 1.59 Å (Ni²⁺) and 2.52 Å (Zn²⁺) resolution, show the conserved proximal and solvent-exposed His¹⁰² residues from two adjacent monomers invariably involved in metal binding. The C-terminal regions of the apoprotein are disordered in the crystal, but acquire significant ordering in the presence of the metal ions due to the binding of His¹⁵². The analysis of X-ray absorption spectral data obtained using solutions of Ni²⁺- and Zn²⁺-bound HpUreE provided accurate information of the metal-ion environment in the absence of solid-state effects. These results reveal the role of the histidine residues at the protein C-terminus in metal-ion binding, and the mutual influence of protein framework and metal-ion stereo-electronic properties in establishing co-ordination number and geometry leading to metal selectivity.

PubMed: 22010876
DOI: 10.1042/BJ20111659

Experimental method

X-RAY DIFFRACTION (2.521 Å)