ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2014
Nickel binding properties of Helicobacter pylori UreF, an accessory protein in the nickel-based activation of urease.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 48 citations in OpenAlex.
- Structural landscape of bacterial urease: implications for catalyst and adaptation.Archives of microbiology · 2026Review
- Anti-urease therapy: a targeted approach to mitigating antibiotic resistance in Helicobacter pylori while preserving the gut microflora.Gut pathogens · 2025Review
- Pyridylpiperazine-based carbodithioates as urease inhibitors: synthesis and biological evaluation.Frontiers in chemistry · 2024Article
- Delivering a toxic metal to the active site of urease.Science advances · 2023Article
- Isolation and pan-genome analysis ofFrontiers in microbiology · 2023Article
- Targeting the Protein Tunnels of the Urease Accessory Complex: A Theoretical Investigation.Molecules (Basel, Switzerland) · 2020Article
- Metabolic functions of the human gut microbiota: the role of metalloenzymes.Natural product reports · 2019Review
- Structural insights into how GTP-dependent conformational changes in a metallochaperone UreG facilitate urease maturation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Aminophosphinates against Helicobacter pylori ureolysis-Biochemical and whole-cell inhibition characteristics.PloS one · 2017Article
- Mutational and Computational Evidence That a Nickel-Transfer Tunnel in UreD Is Used for Activation of Klebsiella aerogenes Urease.Biochemistry · 2015Article
- Intrinsic disorder and metal binding in UreG proteins from Archae hyperthermophiles: GTPase enzymes involved in the activation of Ni(II) dependent urease.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- UreE-UreG complex facilitates nickel transfer and preactivates GTPase of UreG in Helicobacter pylori.The Journal of biological chemistry · 2015Article
- Ca K-edge XAS as a probe of calcium centers in complex systems.Inorganic chemistry · 2015Article
- The conformational response to Zn(II) and Ni(II) binding of Sporosarcina pasteurii UreG, an intrinsically disordered GTPase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Sumner's legacy: a century of urease crystals and recent structural advances.Critical reviews in biochemistry and molecular biologyReview
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7 authors at 3 institutions in 3 countries.
Funding
Abstract
Helicobacter pylori UreF (HpUreF) is involved in the insertion of Ni(2+) in the urease active site. The recombinant protein in solution is a dimer characterized by an extensive α-helical structure and a well-folded tertiary structure. HpUreF binds two Ni(2+) ions per dimer, with a micromolar dissociation constant, as shown by calorimetry. X-ray absorption spectroscopy indicated that the Ni(2+) ions reside in a five-coordinate pyramidal geometry comprising exclusively N/O-donor ligands derived from the protein, including one or two histidine imidazole and carboxylate ligands. Binding of Ni(2+) does not affect the solution properties of the protein. Mutation to alanine of His229 and/or Cys231, a pair of residues located on the protein surface that interact with H. pylori UreD, altered the affinity of the protein for Ni(2+). This result, complemented by the findings from X-ray absorption spectroscopy, indicates that the Ni(2+) binding site involves His229, and that Cys231 has an indirect structural role in metal binding. An in vivo assay of urease activation demonstrated that H229A HpUreF, C231A HpUreF, and H229/C231 HpUreF are significantly less competent in this process, suggesting a role for a Ni(2+) complex with UreF in urease maturation. This hypothesis was supported by calculations revealing the presence of a tunnel that joins the Cys-Pro-His metal binding site on UreG and an opening on the UreD surface, passing through UreF close to His229 and Cys231, in the structure of the H. pylori UreDFG complex. This tunnel could be used to transfer nickel into the urease active site during apoenzyme-to-holoenzyme activation.
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