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

Eva S. Cunha (), Xiaorui Chen, Marta Sanz-Gaitero, Deryck J. Mills and Hartmut Luecke ()
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Eva S. Cunha: University of Oslo and Oslo University Hospital
Xiaorui Chen: University of California
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

Nature Communications, 2021, vol. 12, issue 1, 1-8

Abstract: 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.

Date: 2021
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DOI: 10.1038/s41467-020-20485-6

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