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; Hartmut Luecke

doi:10.1038/s41467-020-20485-6

Nature Communications (Jan 2021)

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,
Hartmut Luecke

Affiliations

Eva S. Cunha: Structural Biology and Drug Discovery Group, Centre for Molecular Medicine Norway, Nordic EMBL Partnership, University of Oslo and Oslo University Hospital
Xiaorui Chen: Department of Molecular Biology and Biochemistry, University of California
Marta Sanz-Gaitero: Structural Biology and Drug Discovery Group, Centre for Molecular Medicine Norway, Nordic EMBL Partnership, University of Oslo and Oslo University Hospital
Deryck J. Mills: Department of Structural Biology, Max Planck Institute of Biophysics
Hartmut Luecke: Structural Biology and Drug Discovery Group, Centre for Molecular Medicine Norway, Nordic EMBL Partnership, University of Oslo and Oslo University Hospital

DOI: https://doi.org/10.1038/s41467-020-20485-6
Journal volume & issue: Vol. 12, no. 1
pp. 1 – 8

Abstract

Read online

Infection by Helicobacter pylori is associated with peptic ulcers and gastric cancer. H. pylori urease is required for colonization of the stomach and thus an attractive antimicrobial drug target. Cryo-EM analyses of the H. pylori urease with inhibitors bound reveal structural details useful in rational drug design.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

About the journal