ArticleBiochemistry2012
Klebsiella aerogenes UreF: identification of the UreG binding site and role in enhancing the fidelity of urease activation.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- Structural landscape of bacterial urease: implications for catalyst and adaptation.Archives of microbiology · 2026Review
- Structural landscape of bacterial urease: implications for catalyst and adaptation.Archives of microbiology · 2026Review
- Delivering a toxic metal to the active site of urease.Science advances · 2023Article
- Structural characterization of the urease accessory protein UreF from Klebsiella pneumoniae.Acta crystallographica. Section F, Structural biology communications · 2022Article
- A Structural Model of the Urease Activation Complex Derived from Ion Mobility-Mass Spectrometry and Integrative Modeling.Structure (London, England : 1993) · 2018Article
- 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
- The assembly of the plant urease activation complex and the essential role of the urease accessory protein G (UreG) in delivery of nickel to urease.The Journal of biological chemistry · 2017Article
- Metallochaperones and metalloregulation in bacteria.Essays in biochemistry · 2017Review
- Expression of an Acid Urease with Urethanase Activity in E. coli and Analysis of Urease Gene.Molecular biotechnology · 2017Review
- 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
- UreE-UreG complex facilitates nickel transfer and preactivates GTPase of UreG in Helicobacter pylori.The Journal of biological chemistry · 2015Article
- 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
- Common themes and unique proteins for the uptake and trafficking of nickel, a metal essential for the virulence of Helicobacter pylori.Frontiers in cellular and infection microbiology · 2013Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Ni-containing active site of Klebsiella aerogenes urease is assembled through the concerted action of the UreD, UreE, UreF, and UreG accessory proteins. UreE functions as a metallochaperone that delivers Ni to a UreD-UreF-UreG complex bound to urease apoprotein, with UreG serving as a GTPase during enzyme activation. This study focuses on the role of UreF, previously proposed to act as a GTPase activating protein (GAP) of UreG. Sixteen conserved UreF surface residues that may play roles in protein-protein interactions were independently changed to Ala. When produced in the context of the entire urease gene cluster, cell-free extracts of nine site-directed mutants had less than 10% of the wild-type urease activity. Enrichment of the variant forms of UreF, as the UreE-F fusion proteins, uniformly resulted in copurification of UreD and urease apoprotein, whereas UreG bound to only a subset of the species. Notably, weakened interaction with UreG correlated with the low-activity mutants. The affected residues in UreF map to a distinct surface on the crystal structure, defining the UreG binding site. In contrast to the hypothesis that UreF is a GAP, the UreD-UreF-UreG-urease apoprotein complex containing K165A UreF exhibited significantly greater levels of GTPase activity than that containing the wild-type protein. Additional studies demonstrated the UreG GTPase activity was largely uncoupled from urease activation for the complex containing this UreF variant. Further experiments with these complexes provided evidence that UreF gates the GTPase activity of UreG to enhance the fidelity of urease metallocenter assembly, especially in the presence of the noncognate metal Zn.
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Registered trials
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.