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

• Published in: Nature communications Vol. 12; no. 1; pp. 230 - 8
• Main Authors: Cunha, Eva S., Chen, Xiaorui, Sanz-Gaitero, Marta, Mills, Deryck J., Luecke, Hartmut
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 11.01.2021; Nature Publishing Group; Nature Portfolio
• Subjects: 101/28; 147/28; 631/154; 631/326/421; 631/45/607/1164; 631/535/1258/1259; Antibiotics; Antiinfectives and antibacterials; Antimicrobial agents; Broadband; Cancer; Catalytic Domain; Clarithromycin; Colonization; Cryoelectron Microscopy; Cytoplasm; Drug development; Electron microscopy; Enzyme Inhibitors - chemistry; Enzyme Inhibitors - pharmacology; Eradication; Gastric cancer; Helicobacter pylori; Helicobacter pylori - enzymology; Humanities and Social Sciences; Hydrogen-Ion Concentration; Infections; Inhibitors; Metronidazole; Models, Molecular; multidisciplinary; Nickel; Peptic ulcers; Proton pump inhibitors; Science; Science (multidisciplinary); Stomach; Therapeutic targets; Ulcers; Urease; Urease - antagonists & inhibitors; Urease - ultrastructure; World population

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, ca...