ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2008
Structure and metal binding properties of ZnuA, a periplasmic zinc transporter from Escherichia coli.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 116 citations in OpenAlex.
- Trial
- Analysis of novel zinc-binding proteins in the cell wall ofJournal of bacteriology · 2025Article
- Prokaryotic mechanosensitive channels mediate copper influx.Protein science : a publication of the Protein Society · 2025Article
- Review
- Identifying potential nutrient acquisition mechanisms for long-term survival: adaptive evolution ofFrontiers in microbiology · 2025Article
- Two zinc ABC transporters contribute toFrontiers in plant science · 2025Article
- Structures, Mechanisms, and Physiological Functions of Zinc Transporters in Different Biological Kingdoms.International journal of molecular sciences · 2024Review
- A bioinformatic analysis of zinc transporters in intestinal Lactobacillaceae.Metallomics : integrated biometal science · 2023Article
- Structure and Function of the Zinc Binding Protein ZrgA fromInternational journal of molecular sciences · 2022Article
- Article
- Conformational flexibility in the zinc solute-binding protein ZnuA.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Contributions of Conformational Flexibility to High-Affinity Zinc Binding in the Solute Binding Protein AztC.ACS omega · 2022Article
- Site 2 of the Yersinia pestis substrate-binding protein YfeA is a dynamic surface metal-binding site.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- A bacterial protease depletes c-MYC and increases survival in mouse models of bladder and colon cancer.Nature biotechnology · 2021Article
- Article
- Conformation of the Solute-Binding Protein AdcAII Influences Zinc Uptake inFrontiers in cellular and infection microbiology · 2021Article
- How Zinc-Binding Systems, Expressed by Human Pathogens, Acquire Zinc from the Colonized Host Environment: A Critical Review on Zincophores.Current medicinal chemistry · 2021Review
- Periplasmic Targets for the Development of Effective Antimicrobials against Gram-Negative Bacteria.ACS infectious diseases · 2020Review
- Structural Features Mediating Zinc Binding and Transfer in the AztABCD Zinc Transporter System.Biomolecules · 2020Article
10 more citing papers are in PubMed but not listed here.
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
ZnuA is the periplasmic Zn(2+)-binding protein associated with the high-affinity ATP-binding cassette ZnuABC transporter from Escherichia coli. Although several structures of ZnuA and its homologs have been determined, details regarding metal ion stoichiometry, affinity, and specificity as well as the mechanism of metal uptake and transfer remain unclear. The crystal structures of E. coli ZnuA (Eco-ZnuA) in the apo, Zn(2+)-bound, and Co(2+)-bound forms have been determined. ZnZnuA binds at least two metal ions. The first, observed previously in other structures, is coordinated tetrahedrally by Glu59, His60, His143, and His207. Replacement of Zn(2+) with Co(2+) results in almost identical coordination geometry at this site. The second metal binding site involves His224 and several yet to be identified residues from the His-rich loop that is unique to Zn(2+) periplasmic metal binding receptors. Electron paramagnetic resonance and X-ray absorption spectroscopic data on CoZnuA provide additional insight into possible residues involved in this second site. The second site is also detected by metal analysis and circular dichroism (CD) titrations. Eco-ZnuA binds Zn(2+) (estimated K (d) < 20 nM), Co(2+), Ni(2+), Cu(2+), Cu(+), and Cd(2+), but not Mn(2+). Finally, conformational changes upon metal binding observed in the crystal structures together with fluorescence and CD data indicate that only Zn(2+) substantially stabilizes ZnuA and might facilitate recognition of ZnuB and subsequent metal transfer.
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