ArticlePLoS biology2013
Structure of UreG/UreF/UreH complex reveals how urease accessory proteins facilitate maturation of Helicobacter pylori urease.
Article in PLoS biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 115 citations in OpenAlex.
- Novel indole-based sulfonate and sulfamate derivatives as potent and selective urease inhibitors targeting Helicobacter pylori: a promising therapeutic strategy.Gut pathogens · 2026Article
- Structural landscape of bacterial urease: implications for catalyst and adaptation.Archives of microbiology · 2026Review
- Unveiling the role of microbial rease in ureolysis-induced calcium carbonate precipitation, Its mechanistic insights, and emerging applications.World journal of microbiology & biotechnology · 2025Review
- Anti-urease therapy: a targeted approach to mitigating antibiotic resistance in Helicobacter pylori while preserving the gut microflora.Gut pathogens · 2025Review
- Amino Acid Complexation Fractionates Nickel Isotopes: Implications for Tracing Nickel Cycling in the Environment.Environmental science & technology letters · 2025Article
- New Directions inInfection and drug resistance · 2025Review
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Protein interactions in human pathogens revealed through deep learning.Nature microbiology · 2024Article
- Epiberberine: a potential rumen microbial urease inhibitor to reduce ammonia release screened by targeting UreG.Applied microbiology and biotechnology · 2024Article
- Article
- Phenotypic Characterization and Draft Genome Sequence Analyses of Two Novel Endospore-FormingMicroorganisms · 2023Article
- The exceptional form and function of the giant bacteriumProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Moving metals: How microbes deliver metal cofactors to metalloproteins.Molecular microbiology · 2023Article
- Delivering a toxic metal to the active site of urease.Science advances · 2023Article
- The structure of the high-affinity nickel-binding site in the Ni,Zn-HypA•UreE2 complex.Metallomics : integrated biometal science · 2023Article
- Structure of metallochaperone in complex with the cobalamin-binding domain of its target mutase provides insight into cofactor delivery.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Novel Copper Oxide Bio-Nanocrystals to Target Outer Membrane Lectin of Vancomycin-ResistantMolecules (Basel, Switzerland) · 2022Article
- Article
- The role of nucleoside triphosphate hydrolase metallochaperones in making metalloenzymes.Metallomics : integrated biometal science · 2022Review
- Structural characterization of the urease accessory protein UreF from Klebsiella pneumoniae.Acta crystallographica. Section F, Structural biology communications · 2022Article
1 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Urease is a metalloenzyme essential for the survival of Helicobacter pylori in acidic gastric environment. Maturation of urease involves carbamylation of Lys219 and insertion of two nickel ions at its active site. This process requires GTP hydrolysis and the formation of a preactivation complex consisting of apo-urease and urease accessory proteins UreF, UreH, and UreG. UreF and UreH form a complex to recruit UreG, which is a SIMIBI class GTPase, to the preactivation complex. We report here the crystal structure of the UreG/UreF/UreH complex, which illustrates how UreF and UreH facilitate dimerization of UreG, and assembles its metal binding site by juxtaposing two invariant Cys66-Pro67-His68 metal binding motif at the interface to form the (UreG/UreF/UreH)2 complex. Interaction studies revealed that addition of nickel and GTP to the UreG/UreF/UreH complex releases a UreG dimer that binds a nickel ion at the dimeric interface. Substitution of Cys66 and His68 with alanine abolishes the formation of the nickel-charged UreG dimer. This nickel-charged UreG dimer can activate urease in vitro in the presence of the UreF/UreH complex. Static light scattering and atomic absorption spectroscopy measurements demonstrated that the nickel-charged UreG dimer, upon GTP hydrolysis, reverts to its monomeric form and releases nickel to urease. Based on our results, we propose a mechanism on how urease accessory proteins facilitate maturation of urease.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.