ArticleThe Journal of biological chemistry2017
Mechanisms of zinc binding to the solute-binding protein AztC and transfer from the metallochaperone AztD.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- Two zinc ABC transporters contribute toFrontiers in plant science · 2025Article
- 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
- Article
- How Zinc-Binding Systems, Expressed by Human Pathogens, Acquire Zinc from the Colonized Host Environment: A Critical Review on Zincophores.Current medicinal chemistry · 2021Review
- Conformation of the Solute-Binding Protein AdcAII Influences Zinc Uptake inFrontiers in cellular and infection microbiology · 2021Article
- Specificity of Interactions between Components of Two Zinc ABC Transporters inInternational journal of molecular sciences · 2020Article
- 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
- Two ABC Transporters and a Periplasmic Metallochaperone Participate in Zinc Acquisition in Paracoccus denitrificans.Biochemistry · 2019Article
- Bioinformatic Exploration of Metal-Binding Proteome of Zoonotic PathogenFrontiers in genetics · 2019Article
- Crystal structures of AztD provide mechanistic insights into direct zinc transfer between proteins.Communications biology · 2019Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Bacteria can acquire the essential metal zinc from extremely zinc-limited environments by using ATP-binding cassette (ABC) transporters. These transporters are critical virulence factors, relying on specific and high-affinity binding of zinc by a periplasmic solute-binding protein (SBP). As such, the mechanisms of zinc binding and release among bacterial SBPs are of considerable interest as antibacterial drug targets. Zinc SBPs are characterized by a flexible loop near the high-affinity zinc-binding site. The function of this structure is not always clear, and its flexibility has thus far prevented structural characterization by X-ray crystallography. Here, we present intact structures for the zinc-specific SBP AztC from the bacterium
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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.