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Structural characterization of binding of Cu(II) to tau protein.
Transition metals have been frequently recognized as risk factors in neurodegenerative disorders, and brain lesions associated with Alzheimer's disease are rich in Fe(III), Zn(II), and Cu(II). ByExpand
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Helicobacter pylori UreE, a urease accessory protein: specific Ni(2+)- and Zn(2+)-binding properties and interaction with its cognate UreG.
The persistence of Helicobacter pylori in the hostile environment of the human stomach is ensured by the activity of urease. The essentiality of Ni(2+) for this enzyme demands proper intracellularExpand
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Zn2+‐linked dimerization of UreG from Helicobacter pylori, a chaperone involved in nickel trafficking and urease activation
The biosynthesis of the active metal‐bound form of the nickel‐dependent enzyme urease involves the formation of a lysine‐carbamate functional group concomitantly with the delivery of two Ni2+ ionsExpand
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Chemistry of Ni2+ in urease: sensing, trafficking, and catalysis.
Transition metals are both essential to enzymatic catalysis and limited in environmental availability. These two biological facts have together driven organisms to evolve mechanisms for selectiveExpand
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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.
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.Expand
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Nickel trafficking: insights into the fold and function of UreE, a urease metallochaperone.
UreE is a metallo-chaperone assisting the incorporation of two adjacent Ni(2+) ions in the active site of urease. This study describes an attempt to distill general information on this protein usingExpand
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The nickel site of Bacillus pasteurii UreE, a urease metallo-chaperone, as revealed by metal-binding studies and X-ray absorption spectroscopy.
UreE is a homodimeric metallo-chaperone that assists the insertion of Ni(2+) ions in the active site of urease. The crystal structures of UreE from Bacillus pasteurii and Klebsiella aerogenes haveExpand
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A model‐based proposal for the role of UreF as a GTPase‐activating protein in the urease active site biosynthesis
UreF is a protein that plays a role in the in vivo urease activation as a chaperone involved in the insertion of two Ni2+ ions in the apo‐urease active site. The molecular details of this process areExpand
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The RNA Hydrolysis and the Cytokinin Binding Activities of PR-10 Proteins Are Differently Performed by Two Isoforms of the Pru p 1 Peach Major Allergen and Are Possibly Functionally Related[W]
PR-10 proteins are a family of pathogenesis-related (PR) allergenic proteins playing multifunctional roles. The peach (Prunus persica) major allergen, Pru p 1.01, and its isoform, Pru p 1.06D, wereExpand
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UreG, a Chaperone in the Urease Assembly Process, Is an Intrinsically Unstructured GTPase That Specifically Binds Zn2+*
Bacillus pasteurii UreG, a chaperone involved in the urease active site assembly, was overexpressed in Escherichia coli BL21(DE3) and purified to homogeneity. The identity of the recombinant proteinExpand
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