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Journal Article

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


Mills,  Deryck J.
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Cunha, E. S., Chen, X., Sanz-Gaitero, M., Mills, D. J., & Luecke, H. (2021). Cryo-EM structure of Helicobacter pylori urease with an inhibitor in the active site at 2.0 Å resolution. Nature Communications, 12(1): 230. doi:10.1038/s41467-020-20485-6.

Cite as: http://hdl.handle.net/21.11116/0000-0007-AD2F-3
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.