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Cryo-EM structure of Helicobacter pylori urease with an inhibitor in the active site at 2.0 Å resolution

Author

Listed:
  • Eva S. Cunha

    (University of Oslo and Oslo University Hospital)

  • Xiaorui Chen

    (University of California
    Genomics Research Center, Academia Sinica)

  • Marta Sanz-Gaitero

    (University of Oslo and Oslo University Hospital)

  • Deryck J. Mills

    (Max Planck Institute of Biophysics)

  • Hartmut Luecke

    (University of Oslo and Oslo University Hospital
    University of California
    University of Oslo and Oslo University Hospital
    University of California)

Abstract

Infection of the human stomach by Helicobacter pylori remains a worldwide problem and greatly contributes to peptic ulcer disease and gastric cancer. Without active intervention approximately 50% of the world population will continue to be infected with this gastric pathogen. Current eradication, called triple therapy, entails a proton-pump inhibitor and two broadband antibiotics, however resistance to either clarithromycin or metronidazole is greater than 25% and rising. Therefore, there is an urgent need for a targeted, high-specificity eradication drug. Gastric infection by H. pylori depends on the expression of a nickel-dependent urease in the cytoplasm of the bacteria. Here, we report the 2.0 Å resolution structure of the 1.1 MDa urease in complex with an inhibitor by cryo-electron microscopy and compare it to a β-mercaptoethanol-inhibited structure at 2.5 Å resolution. The structural information is of sufficient detail to aid in the development of inhibitors with high specificity and affinity.

Suggested Citation

  • Eva S. Cunha & Xiaorui Chen & Marta Sanz-Gaitero & Deryck J. Mills & Hartmut Luecke, 2021. "Cryo-EM structure of Helicobacter pylori urease with an inhibitor in the active site at 2.0 Å resolution," Nature Communications, Nature, vol. 12(1), pages 1-8, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-020-20485-6
    DOI: 10.1038/s41467-020-20485-6
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    Cited by:

    1. Diana Evstafeva & Filip Ilievski & Yinyin Bao & Zhi Luo & Boris Abramovic & Sunghyun Kang & Christian Steuer & Elita Montanari & Tommaso Casalini & Dunja Simicic & Dario Sessa & Stefanita-Octavian Mit, 2024. "Inhibition of urease-mediated ammonia production by 2-octynohydroxamic acid in hepatic encephalopathy," Nature Communications, Nature, vol. 15(1), pages 1-17, December.

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