ArticleProteins2010
Crystal structure of a truncated urease accessory protein UreF from Helicobacter pylori.
Article in Proteins, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 42 citations in OpenAlex.
- Anti-urease therapy: a targeted approach to mitigating antibiotic resistance in Helicobacter pylori while preserving the gut microflora.Gut pathogens · 2025Review
- Structural characterization of the urease accessory protein UreF from Klebsiella pneumoniae.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Targeting the Protein Tunnels of the Urease Accessory Complex: A Theoretical Investigation.Molecules (Basel, Switzerland) · 2020Article
- Mutational and Computational Evidence That a Nickel-Transfer Tunnel in UreD Is Used for Activation of Klebsiella aerogenes Urease.Biochemistry · 2015Article
- Evolution of Macromolecular Docking Techniques: The Case Study of Nickel and Iron Metabolism in Pathogenic Bacteria.Molecules (Basel, Switzerland) · 2015Review
- 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
- 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
- Nickel binding properties of Helicobacter pylori UreF, an accessory protein in the nickel-based activation of urease.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Structure of UreG/UreF/UreH complex reveals how urease accessory proteins facilitate maturation of Helicobacter pylori urease.PLoS biology · 2013Article
- Analysis of a soluble (UreD:UreF:UreG)2 accessory protein complex and its interactions with Klebsiella aerogenes urease by mass spectrometry.Journal of the American Society for Mass Spectrometry · 2013Article
- Structure of the UreD-UreF-UreG-UreE complex in Helicobacter pylori: a model study.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
- Biosynthesis of the urease metallocenter.The Journal of biological chemistry · 2013Review
- Cofactor biosynthesis through protein post-translational modification.Current opinion in chemical biology · 2012Review
- Klebsiella aerogenes UreF: identification of the UreG binding site and role in enhancing the fidelity of urease activation.Biochemistry · 2012Article
- Unraveling the Helicobacter pylori UreG zinc binding site using X-ray absorption spectroscopy (XAS) and structural modeling.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012Article
- Assembly of preactivation complex for urease maturation in Helicobacter pylori: crystal structure of UreF-UreH protein complex.The Journal of biological chemistry · 2011Article
- Function of UreB in Klebsiella aerogenes urease.Biochemistry · 2011Article
- Mutational analysis of the major soybean UreF paralogue involved in urease activation.Journal of experimental botany · 2011Article
- Sumner's legacy: a century of urease crystals and recent structural advances.Critical reviews in biochemistry and molecular biologyReview
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Urease plays a central role in the pathogenesis of Helicobacter pylori in humans. Maturation of this nickel metalloenzyme in bacteria requires the participation of the accessory proteins UreD (termed UreH in H. pylori), UreF, and UreG, which form sequential complexes with the urease apoprotein as well as UreE, a metallochaperone. Here, we describe the crystal structure of C-terminal truncated UreF from H. pylori (residues 1-233), the first UreF structure to be determined, at 1.55 A resolution using SAD methods. UreF forms a dimer in vitro and adopts an all-helical fold congruent with secondary structure prediction. On the basis of evolutionary conservation analysis, the structure reveals a probable binding surface for interaction with other urease components as well as key conserved residues of potential functional relevance.
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