ArticleThe Journal of biological chemistry2022
The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 9 citations in OpenAlex.
- A redox- and proton-coupled inner membrane transporter mediates copper import to the bacterial cytoplasm.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Navigating the copper highway: bacterial strategies for cytoplasmic import.Journal of inorganic biochemistry · 2026Review
- A critical role of copper homeostasis in the virulence of Klebsiella pneumoniae.Communications biology · 2025Article
- The Escherichia coli AZY operon links copper uptake to antibiotic resistance.Communications biology · 2025Article
- Insights into bacterial metabolism from small RNAs.Cell chemical biology · 2024Review
- Unique underlying principles shaping copper homeostasis networks.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
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Authors and funding
9 authors at 4 institutions in 2 countries.
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Abstract
The Escherichia coli yobA-yebZ-yebY (AZY) operon encodes the proteins YobA, YebZ, and YebY. YobA and YebZ are homologs of the CopC periplasmic copper-binding protein and the CopD putative copper importer, respectively, whereas YebY belongs to the uncharacterized Domain of Unknown Function 2511 family. Despite numerous studies of E. coli copper homeostasis and the existence of the AZY operon in a range of bacteria, the operon's proteins and their functional roles have not been explored. In this study, we present the first biochemical and functional studies of the AZY proteins. Biochemical characterization and structural modeling indicate that YobA binds a single Cu
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